Crystal structure of the ligand binding domain of the retinoic acid-related orphan receptor alpha (ror-alpha)

ABSTRACT

The present invention relates RORa in crystallized form and methods for the preparation thereof. The invention also provides a three-dimensional model of RORa and means for the design of RORa modulators. Ligands binding to RORa are also provided.

FIELD OF THE INVENTION

The present invention relates RORα in crystallized form and methods for the preparation thereof. The invention further provides a three-dimensional model of RORα and means for the design of RORα modulators.

BACKGROUND OF THE INVENTION

The retinoic acid-related orphan receptor α (RORα) is an orphan member of nuclear receptor protein family to which belong receptors such as retinoic acid receptor (RAR), peroxisome proliferator-activated receptor (PPAR), estrogen receptor (ER), vitamin D receptor (VDR) and thyroid receptor (TR). Like other members of the nuclear receptor family, RORα exhibits a modular structure composed of several domains, among them a DNA-binding domain (DBD) and a ligand-binding domain (LBD). The latter displays low degree of homology with the LBD of T3Rβ (25%), VDR (24%), RARα (24%), PPARα (24%) and RXRα (20%) from which X-ray structures have been solved. However, attempts to crystallize the LBD of RORα have failed so far and no X-ray structure of RORα was available. In addition, to this point, no ligand has been identified until now. Our understaniding of the physiological role of the receptor would be greatly enhanced by the discovery of a natural ligand. Further, provision of the spatial organization would assist in the designing of agonists and antagonists of RORα.

SUMMARY OF THE INVENTION

In one aspect, the present invention provides crystalline LBD of RORα. In a related aspect the invention provides crystalline LBD of RORα associated with a ligand.

In another aspect, the invention provides a set of co-ordinates representing the spatial organization of the LBD of RORα. In a related aspect the invention provides a model of the LBD of RORα comprising a set of co-ordinates embodying the structure of the LBD of RORα. In another related aspect, this invention provides for a set of co-ordinates useful in drug design. In yet another related aspect, the invention provides for a method for identifying a substance binding to the LBD of RORα, comprising providing a model embodying the structure of the LBD of RORα, assessing the interaction of a candidate substance with said model, and selecting a substance which is predicted to interact with the LBD of RORα Substances identified by this method are also provided.

In a further aspect, the invention provides for a method for identifying a compound acting as agonist or antagonist of RORα that binds to the LBD of RORα comprising selecting a potential compound by performing rational drug design with one or more sets of atomic coordinates embodying the structure of the LBD of RORα, contacting the potential compound with a LBD of RORα and measuring the binding of the compound to the LBD of RORα. Agonists and antagonists identified by this method are also provided.

In another aspect, the present invention provides for a method of screening for compounds interacting with RORα comprising contacting RORα with a candidate compound, measuring interactions between the candidate compound and RORα in the absence of sterols, and selecting said compound if it interacts with RORα in the absence of sterols. Preferred sterols are cholesterol or cholesterol derivatives. Compounds identified by this method are also provided.

In another aspect of the present invention, the use of RORα for the screening of cholesterol related diseases is provided.

In yet another aspect the present invention provides a composition comprising LBD of RORα and a sterol, preferably cholesterol or a cholesterol derivative. In a preferred embodiment, said composition is crystallizable.

BRIEF DESCRIPTION OF THE TABLES AND FIGURES

Table 1: Native crystal data and X-ray data statistics of LBD of RORα in complex with cholesterol.

Table 2: Hg-derivative crystal data, X-ray data and heavy atom refinement statistics (for complex with cholesterol).

Table 3: Refinement statistics (for complex with cholesterol).

Table 4: shows effects of mutations preventing binding of cholesterol to RORα.

Table 5: shows effects of fluvastatin on RORα transcriptional activity.

Table 6: Effect of cholesterol and cholesterol derivative on ROR alpha transcriptional activity.

Table 7: Native crystal data and refinement statistics of LBD of RORα in complex with cholesterol sulfate.

Table 8: Atomic structure coordinates for a representative structure of the LBD of RORα in complex with cholesterol (numbering according to Swissprot P35398-1).

Table 9: Atomic structure coordinates for a representative structure of the LBD of RORα in complex with cholesterol-sulfate (numbering according to Swissprot P35398-2).

FIG. 1: Sequence of human RORα (Swissprot P35398-1).

FIG. 2 shows a schematic representation of the X-ray structure of the complex between RORα-LBD and cholesterol.

FIG. 3 shows a zoomed in view of the complex between RORα-LBD and cholesterol (numbering according to Swissprot P35398-1).

FIG. 4: Proposal of ligands in order to increase the affinity and to obtain antagonistic activity (numbering according to Swissprot P35398-1).

FIG. 5: Proposal of further derivatives of cholesterol in order to increase the affinity (numbering according to Swissprot P35398-1).

FIG. 6 shows the displacement of cholesterol by 25-OH cholesterol and cholesterol sulfate.

FIG. 7 shows a zoomed view of X-ray structure of ROR(alpha)/cholesterol (numbering according to Swissprot P35398-2).

FIG. 8 Overview of interactions made by cholesterol-sulfate with LBP of ROR(alpha) (numbering according to Swissprot P35398-2).

FIG. 9 Comparison of the X-ray structures of ROR(alpha)/cholesterol-sulfate and ROR(alpha)/cholesterol (numbering according to Swissprot P35398-2).

FIG. 10 Comparison of the X-ray structures of ROR(alpha)/cholesterol (left) and ROR(alpha)/cholesterol-sulfate (right) (numbering according to Swissprot P35398-2).

FIG. 11 Sequence of the construct used in crystallization. The secondary structure elements are shown below the sequence. Amino acids that have a nonhydrogen atom closer than 4 Å to cholesterol are highlighted in red (numbering according to Swissprot P35398-2).

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides crystals of the LBD of RORα. Moreover, the present invention provides the structural determination of such crystals by X-ray crystallography. In one embodiment, the structure of the crystal has been solved to a resolution of 1.88 Å. Surprisingly, it was found that the crystal contained a ligand associated to RORα. The ligand was identified as cholest-5-en-3beta-ol (cholesterol). Thus the present invention not only provides information on the spatial organization of the LBD of RORα useful for instance for in-silico screening, docking and rational drug design, but also cholesterol as a ligand binding to the RORα which is useful for the identification of amino acids involved in the ligand binding. The information provided in accordance with the present invention can be used as basis for the design of compounds binding to the LBD of RORα, as exemplified below. The crystal LBD of RORα provided by this invention can take any crystalline form, but is preferably a single crystal. In a more preferred embodiment the crystal comprises a unit cell having the of a=55 Å±5 Å, b=50 Å±5 Å, c=60 Å±6 Å and β=98.5°±9° and space group P2₁. Preferably, the unit cell dimensions are a=55.9 Å±2 Å, b=49.9 Å±2 Å, c=60.7 Å±2 Å and β=98.7°±5° or a=54.4 Å±2 Å, b=49.9 Å±2 Å, c=60.7 Å±2 Å, β=97.8°±5°. In another preferred embodiment, the crystalline LBD of RORα is of human origin. The crystalline LBD of RORα according to the present invention is preferably associated with a second chemical substance. Such a substance may be any natural or synthetic chemical molecule, preferred are small molecules, more preferred are small lipophilic molecules. Cholesterol has been identified, in accordance with the present invention, as a ligand fitting into this binding pocket. Thus, in a particularly preferred embodiment such a substance is cholesterol or a cholesterol derivative. As used herein, the term “small molecule” refers to a natural or synthetic compound, preferably an organic molecule, with a molecular weight less than 3000 Da, more preferably less than 1000 Da, most preferably less than 500 Da. The term “lipophilic”, as used herein, refers to compounds that are mainly unpolar and that are not or only slightly soluble in water. Typical examples may include fatty acids, retinoic acids, melatonin, steroid hormones, vitamin D derivatives. Other examples may include lipophilic molecules like tamoxifen or raloxifen. In accordance with the present invention, a particularly preferred lipophilic ligand is cholesterol and derivatives thereof. As used herein the term “cholesterol derivative” means a molecule that possesses similarity to cholesterol, such as the same overall structure, but with different substituents or differences in the location of unsaturated bonds or sterical isomers. Examples for such cholesterol derivatives can for instance be found in http://www.steraloids.com.

Crystals of the LBD of RORα and, optionally a second chemical species can be grown by a number of techniques including batch crystallization, vapor diffusion (either by sitting drop or hanging drop) and by microdialysis. Seeding of the crystals in some instances is required to obtain X-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used. An initial crystal can be allowed to grow over several weeksat 4° C. or at room temperature (ca. 20° C.) from a hanging drop. Crystals then can be subsequently grown by macroseeding from the initial crystal. Once a crystal of the present invention is grown, X-ray diffraction data can be collected. A MAR imaging plate detector for X- ray diffraction data collection can be used for example. Crystals can be characterized by using X-rays produced in a conventional source (such as a sealed tube or a rotating anode) or using a synchrotron source.

Methods of characterization and data collection include, but are not limited to, precession photography, oscillation/rotation data collection and diffractometer data collection. As exemplified below, heavy atom derivatives can be obtained by soaking crystals in solution with 4 mM methylmercuric acetate for 1 hour. Data processing and reduction can be carried out using programs (DENZO, and SCALEPACK) of the HKL-suite [Otwinowski and Minor, Meth. Enzymol. 276:307-326 (1997)]. Heavy atom positions can be found using programs such as SnB [Weeks, C. M. & Miller, R. (1999) J.Appl.Cryst.32, 120-124.] or programs (e.g. SHELX and RSPS) of the CCP4 program suite [Collaborative Computational Project, Number4, Acta Cryst. D53: 760-763 (1994)]. Electron density maps can be calculated using programs (e.g. MLPHARE and DM) of the CCP4 program suite [Collaborative Computational Project, Number4, Acta Cryst. D53: 760-763 (1994)] or alternatively using SHARP [La Fortelle, E. D. and Bricogne, G., Methods in Enzymology 276:472-494 1997)] and SOLOMON. Molecular models can be built into this map using O [Jones, T. a. et al., ACTA Crystallogr. A47:110-119 (1991)]. A complete molecular model for the protein can be built on the basis of the experimental electron density map. Model building interspersed with positional and simulated annealing refinement using X-PLOR, (Brunger, X-PLOR v.3.1 Manual, New Haven: Yale University, (1993)] or with CNS, using a maximum likelihood residual [Brunger, A. T. et al., Acta Cryst. D54: 905-921 (1998)] can permit an unambiguous trace and sequence assignment of the LBD of RORα.

Accordingly, the present invention provides for a model of the structure of the LBD of RORα useful for rational drug design comprising a set of co-ordinates embodying the structure of the LBD of RORα. Thus, a preferred embodiment provides for a model embodying the structure of the LBD RORα comprising one or more sets of atomic coordinates in Table 8 or 9. Other preferred embodiments provide a computer system comprising computer hardware or the model of the present invention and a computer readable medium comprising the model of the present invention. The set of co-ordinates is preferably determined by crystallographic analysis of the LBD of RORα, however any available method may be used to construct such a model using data disclosed herein or obtained from independent crystallographic analysis of the LBD of RORα. The term “structure co-ordinates” refers to Cartesian co-ordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a protein or protein-ligand complex in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the enzyme or enzyme complex. Variations in co-ordinates may be generated because of mathematical manipulations of the structure co-ordinates. For example, the structure co-ordinates set forth in Table 8 or 9 could be manipulated by crystallographic permutations of the structure co-ordinates, fractionalization of the structure co-ordinates, integer additions or subtractions to sets of the structure co-ordinates, inversion of the structure co-ordinates or any combination of the above. Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in structure co-ordinates. If such variations are within an acceptable standard error as compared to the original co-ordinates, the resulting three-dimensional shape is considered to be the same. Various computational analyses are therefore necessary to determine whether a molecule or molecular complex or a portion thereof is sufficiently similar to all or parts of the structure of the LBD of RORα as to be considered the same. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1, and as described in the accompanying User's Guide. For the purpose of this invention, any molecule or molecular complex that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than 1.5 Å; when superimposed on the relevant backbone atoms described by structure co-ordinates listed in Table 8 or 9 are considered identical. More preferably, the root mean square deviation is less than 1.0 Å. The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean. It is a way to express the deviation or variation from a trend or object. For purposes of this invention, the “root mean square deviation” defines the variation in the backbone of a protein or protein ligand complex from the relevant portion of the backbone of the LBD of RORα as defined by the structure co-ordinates described herein.

In certain embodiments, the data set embodies a portion of the structure of the LBD of RORα, including without limitation the binding pocket of LBD of RORα. The term “binding pocket”, as used herein, refers to a region of a molecule or molecular complex, that, as a result of its shape, favorably associates with another chemical entity or compound. In accordance with the present invention, a preferred binding pocket includes the amino acids shown in FIGS. 3, 4, 5, 7, 8, 9 or 10 one or more of the following amino acids: Cys321, Gln322, Tyr323, Leu328,Trp353, Cys356, Ala357, Lys359, Ile360, Glu362, Ala363, Val397, Phe398, Arg400, Met4, Arg403, Ala404, Val412, Tyr413, Phe414, Phe424, Leu427, Cys429, Phe432, Ile433, Val436, His517, Lys520 and Tyr540 (numbering according to SWISS-PROT P35398-1).

In one embodiment of the present invention, the model may be used to identify substances that interact with the LBD of RORα. In general, molecular similarity applications in accordance with the present invention permit comparisons between different structures, different conformations of the same structure, and different parts of the same structure. A potential interacting substance is examined through the use of computer modeling using a docking program such as GRAM, DOCK, or AUTODOCK [Dunbrack et al., Folding & Design, 2:27-42 (1997)]. This procedure can include computer fitting of potential ligands to the LBD of RORα, for example to ascertain how well the shape and the chemical structure of the potential ligand will complement with the binding pocked provided by the present application. Computer programs can also be employed to estimate the attraction, repulsion, and steric hindrance of the ligand to the LBD of RORα. Generally the tighter the fit (e.g., the lower the steric hindrance, and/or the greater the attractive force) the more potent the potential drug will be since these properties are consistent with a tighter binding constant. Furthermore, the more specificity in the design of a potential drug the more likely that the drug will not interfere with other properties of the RORα protein or other proteins (particularly proteins present in the nucleus). This will minimize potential side-effects due to unwanted interactions with other proteins. Initially a potential interacting substance could be obtained by screening a chemical library. A ligand selected in this manner could then be systematically modified by computer modeling programs until one or more promising potential ligands are identified. Alternatively, a known ligand of RORα, such as for instance cholesterol as identified in accordance with this invention, may be used as a starting point for systematic modification. Such computer modeling allows the selection of a finite number of rational chemical modifications, as opposed to the countless number of essentially random chemical modifications that could be made, and of which any one might lead to a useful drug. Each chemical modification requires additional chemical steps, which while being reasonable for the synthesis of a finite number of compounds, quickly becomes overwhelming if all possible modifications needed to be synthesized. Thus through the use of the three-dimensional structures disclosed herein and computer modeling, a large number of these compounds can be rapidly screened on the computer monitor screen, and a few likely candidates can be determined without the laborious synthesis of untold numbers of compounds.

Accordingly, methods for identifying substances that bind to the LBD of RORα are provided. Such methods typically include the steps of providing a model embodying the structure of the LBD of RORα, assessing the interaction of a candidate substance with said model, selecting a substance which is predicted to interact with the LBD of RORα, and, optionally, contacting the selected substance with the LBD of RORα. In a preferred embodiment, such a method includes comparing the 3-D structure of candidate compounds with the 3-D molecular model shown in Table 8 or 9 or with the co-ordinates of amino acids which are part of a preferred binding pocket or directly or indirectly involved in binding of a ligand, as herein disclosed for instance in FIGS. 3, 4, 5, 7, 8, 9 or 10. Preferably, said amino acids can form hydrogen bonds with hydrogen bonding functional groups (directly or via water molecules) in a candidate compound or can form favorable vdW-interactions. The interactions are preferably assessed by a computer-assisted method, such as for instance a data processing method in which the structure co-ordinate data as described above is input in a data structure such that the interatomic distances between the atoms of the LBD of RORα are easily retrieved, and the distances between hydrogen-bonding functional groups of different candidate compounds and hydrogen bonding atoms of the amino acids that form the binding pocket in the 3D molecular model are compared (or the distances between groups forming vdW-interactions) thereby allowing the identification of those candidate compounds which would theoretically form the most stable complexes with the 3-D molecular model binding pocket of the LBD of RORα, based on optimal hydrogen bonding and vdW-interactions between the two structures.

In a preferred embodiment the substances are designed to interact via vdW-interactions or via hydrogen bond interactions directly or indirectly (e.g. via water molecules) with atoms of one or more amino acids shown in FIGS. 3, 4, 5, 7, 8, 9 or 10 or selected from the group consisting of Cys321, Gln322, Tyr323, Leu328,Trp353, Cys356, Ala357, Lys359, Ile360, Glu362, Ala363, Val397, Phe398, Arg400, Met401, Arg403, Ala404, Val412, Tyr413, Phe414, Phe424, Leu427, Cys429, Phe432, Ile433, Val436, His517, Lys520 and Tyr540, Gln322, Tyr323, Arg400, Arg403. In a more preferred embodiment the substances interact via vdW-interactions or via hydrogen bond interactions directly or indirectly (e.g. via water molecules) with atoms of one or more amino acids selected from the group consisting of Gln322, Tyr323, Arg400, Arg403 or Trp353, Lys359, Ile360, Ala363, Met401, Phe414, Leu427, Phe432, Val436. Substances identified using the above methods are also provided. Preferred substances are small molecules, more preferred are small lipophilic molecules (possibly with a polar group) and particularly preferred are cholesterol or cholesterol derivatives, such as for instance cholesterol sulfate. In a further preferred embodiment, the binding constant of the substance to RORα is at least 1 μM, preferably at least 100 nM, more preferably at least 10 nM.

In addition, agonists and antagonists of RORα are provided. In one embodiment methods for screening for agonists or antagonists of RORα are provided. Such methods include selecting a potential agonistic or antagonistic compound by performing rational drug design with one or more sets of atomic co-ordinates embodying the structure of the LBD of RORα, contacting the potential compound with a LBD of RORα and measuring the biological activity of RORα. The selection is typically made in conjunction with computer modeling. A potential compound is identified as agonist if it increases the biological activity of RORα or as antagonist if it decreases the biological activity of RORα. Agonists and antagonists identified by such methods are also provided. The agonist or antagonist needs not to bind to the binding pocket used by the natural ligand of RORα, but could also bind at another position and exert its effect allosterically. A preferred embodiment of an agonist according to the present invention is a compound that stabilizes helix 12 (H12) in the agonistic position, i.e. the position in which H12, together with the H3-H4 region, forms the proper interaction surface, i.e. the complete AF-2, for the coactivator (reviewed e.g. in Renaud & Moras, Cell. Mol. Life Sci., 57, 1748-1769, 2000). A preferred embodiment of an antagonist according to the present invention is a compound that destabilizes the agonistic position of H12 for instance by tilting the position of H12 (reviewed e.g. in Renaud & Moras, 2000, supra). Destabilisation of H12 may for instance be achieved by a cholesterol derivative with a bulky substituent at position 26 thus displacing Tyr540 and/or His517. In a preferred embodiment such agonists or antagonists are small molecules. Particularly preferred are lipophilic small molecules. Examples without being limiting are for instance fatty acids, retinoic acids, melatonin, steroid hormones, vitamin D derivatives, but also compounds similar to tamoxifen or raloxifen or derivatives thereof. In one embodiment, such agonists or antagonists may be cholesterol or cholesterol derivatives. In a preferred embodiment of this invention the cholesterol ligand has been modified using the structural information provided by the present invention to a cholesterol derivative binding more strongly to the ligand binding pocked (LBP) of the LBD of RORα provided by the present invention. An example for a more strongly, competitively binding cholesterol derivative that has been designed using the structural information provided by this invention is cholesterol sulfate (see below). In another preferred embodiment, the present invention provides a pharmaceutical composition comprising a therapeutically effective amount of a compound stabilizing H12 of RORα in an agonistic position and a pharmaceutically acceptable carrier. In a related embodiment, the present invention provides a pharmaceutical composition comprising a therapeutically effective amount of a compound destabilizing H12 of RORα in an agonistic position and a pharmaceutically acceptable carrier.

Once a potentially binding substance, such as an agonist or antagonist, is identified it can be either selected from a library of chemicals or alternatively the potential ligand may be synthesized de novo. The de novo synthesis of one or even a relatively small group of specific compounds is reasonable in the art of drug design. The prospective drug can be placed into any standard binding assay to test its effect on any particular RORα function, for instance on the DNA binding of RORα exemplified below. When a suitable drug is identified, a supplemental crystal can be grown which comprises a protein-ligand complex, for instance formed between the binding pocket of the LBD of RORα and the drug. Preferably the crystal effectively diffracts X-rays allowing the determination of the atomic co-ordinates of the protein-ligand complex to a resolution of greater than 5.0 Angstroms, more preferably greater than 3.0 Angstroms or greater than 2.0 Angstroms. The three-dimensional structure of the supplemental crystal can be determined by molecular replacement analysis. Molecular replacement involves using a known three-dimensional structure as a search model to determine the structure of a closely related molecule or protein-ligand complex in a new crystal form. The measured X-ray diffraction properties of the new crystal are compared with the search model structure to compute the position and orientation of the protein in the new crystal. Computer programs that can be used include: programs (AMORE, MOLREP) of the CCP4 program suite [Collaborative Computational Project, Number4, Acta Cryst. D53: 760-763 (1994)] or X-PLOR [Brunger, X-PLOR v.3.1 Manual, New Haven: Yale University, (1993)]. Once the position and orientation are known an electron density map can be calculated using the search model to provide X-ray phases. Thereafter, the electron density is inspected for structural differences and the search model is modified to conform to the new structure. Using this approach, it will be possible to use the claimed structure to solve the three-dimensional structures of any such LBD of RORα complex. For all of the drug screening assays described herein further refinements to the structure of the drug will generally be necessary and can be made by the successive iterations of any and/or all of the steps provided by the particular drug screening assay.

The substances identified by rational design can be further analyzed in drug screening assay. The drug screening assays of the present invention may use any of a number of assays for measuring the functionality of RORα, including for the ability of RORα following ligand binding to transcriptionally regulate a gene, by increasing phosphorylation of RORα, by allowing RORα to dimerize or to heterodimerize with another nuclear receptor, by improving its ability to interact with co-activators, by changing its conformation and by increasing its ability to bind DNA. In one binding assay, a nucleic acid containing a RORα binding site is placed on a coated or onto a solid support. A preferred binding site is a response element (RORE) composed of a 6 bp AT rich motif immediately preceding a half site AGGTCA and the possible variants of this response element that are given in Giguere et al. 1994, Genes & Development 8:538-553, Mc Broom et al. 1995 Mol.Cell. Biol. 15: 796-808, Moraitis & Giguere, 1999; Molecular Endocrinology. 13:431-439. Methods for placing the nucleic acid on the solid support are well known in the art and include linking biotin to the nucleic acid and linking avidin to the solid support. The RORα is allowed to equilibrate with the nucleic acid and drugs are tested to see if they disrupt or enhance the binding.

In another assay, a co-activator protein, such as for instance GRIP or DRIP 205 (Brandon-Atkins et al. 1999, Molecular Endocrinology 13: 1550-1557), or SRC1, NcoA-1, ERAP/P160, SRC2/NcoA-2, ACTR, SRC-3, pCIP, ERAP-140, RIP 140, RIP 160 P/Caf, CBP/P), ARA70, Ada 3, Rap 46, GRIP170, TRIP 1, PGC1 and 2, SPT6, TIFα, SW1/SNUERF, TRAP 100, TRAP 220, DRIP, NSD1 (Robyr et al. 2000, Mol. Endo. 14: 329-347), are placed on a coated or onto a solid support The RORα protein may be labeled. For example, in one embodiment radiolabeled RORα proteins are used to measure the effect of a drug on binding. In another embodiment the natural ultraviolet absorbance of the RORα protein is used. In yet another embodiment, a Biacore chip (Pharmacia) coated with the co-activator peptide is used and the change in surface conductivity can be measured. In yet another embodiment, the effect of a prospective drug (a candidate compound) on interactions between RORα and their DNA binding sites are assayed in living cells that contain or can be induced to contain activated RORα proteins. Cells containing a reporter gene, such as the heterologous gene for luciferase, green fluorescent protein, chloramphenicol acetyl transferase or 3-galactosidase and the like are operably linked to a promoter containing a RORα binding site. A prospective drug is then contacted with the cell. The amount (and/or activity) of reporter produced in the absence and presence of prospective drug is determined and compared. Prospective drugs which reduce the amount (and/or activity) of reporter produced are candidate antagonists of the RORα DNA binding, whereas prospective drugs which increase the amount (and/or activity) of reporter produced are candidate agonists of RORα DNA binding. Assays for detecting the reporter gene products are readily available in the literature. For example, luciferase assays can be performed according to the manufacturer's protocol (Promega), and beta-galactosidase assays can be performed as described by Ausubel et al., [in Current Protocols in Molecular Biology, J. Wiley & Sons, Inc. (1994)]. In one example, the transfection reaction can comprise the transfection of a cell with a plasmid modified to contain a RORα protein.

In one embodiment, the prospective drugs identified by the methods of this invention can be tested for pharmacological activity using assays known in the art. For example, the identified prospective drugs can be tested for activity as potential drugs for the prophylaxis or treatment of a disease or medical condition which involves excessive bone or cartilage loss using a method as disclosed in WO 01/26737. For instance, a reporter assay can be carried out using the bone sialoprotein (BSP) or osteocalcin (OC), which are known modulators of bone mineralization and remodelling. Suitable cells can be transfected with a reporter construct in which a BSP or an OC promoter drive a reporter gene, such as the firefly luciferase gene. A prospective drug is then contacted with the cell. The amount of luciferase activity produced in the absence and presence of prospective drug is determined and compared. In another embodiment, the system for testing prospective drugs according to the present invention can be the use of classical ovariectomized rat model, the loss of ovarian function induces a drop in circulating estrogen promptly followed by decrease of bone mass (Wronski et al., Calcified Tissue International. 45(6):360, 1989). The drug will be tested on ovariectomized animal for a curative treatment of 8 weeks started twelve weeks after ovariectomy and bone mineral density will be monitored. Another type of experiment could be envisaged which is a preventive treatment of intact animals for eight weeks.

Cholesterol has been found to be a ligand of RORα. In accordance with this finding, the present invention provides novel assay methods for the identification of compounds binding to RORα, in particular for the identification of compounds modulating RORα activity, wherein interactions between the candidate compounds and RORα are allowed to take place in a surrounding reduced in cholesterol, preferably free of cholesterol. Such a method typically includes the steps of (a) contacting RORα with a candidate compound, (b) measuring interactions between the candidate compound and RORα in a surrounding essentially free of cholesterol, and (c) selecting said compound if it interacts with RORα. Though not a requirement, it is preferred that all method-steps are carried out in the cholesterol-reduced, or preferably essentially cholesterol-free, surrounding. In a more preferred embodiment, such a method relates to a eukaryotic cellular system. In a yet even more preferred embodiment insect cells are used. Insect cells differ from eukaryotic cells by lacking the capacity for de novo sterol synthesis. It has been shown that these cells can be propagated under cholesterol-free conditions (Cleverley et al. 1997, Exp. Cell Res. 233: 288-296). Thus, such a cell system could for instance provide an appropriate cell background to monitor the activity of a RORα ligand using the RORα cloned in an appropriate insect cell vector and the classical reporter ROREtkluc. In another embodiment, eukaryotic cells, preferably human cells, are used. These cells can for instance be cultured in medium essentially free of cholesterol and in serum essentially free of LDL-cholesterol (the LDL-free serum preparation is described in Goldstein et al 1983, Methods in Enzymology 98:241-260). Mammalian cells are able to produce cholesterol endogenously. The meaning of essentially cholesterol-free surrounding according to the present invention does not include such endogenously produced cholesterol. In a particular embodiment, endogenously cholesterol producing mammalian cells could for instance be used in an assay to screen the ability of a compound to displace endogenous cholesterol.

Nuclear receptors are known to regulate the transcription of specific genes or sets of genes upon ligand binding, which makes them interesting targets for the screening for compounds useful as therapeutics. So far, however, deeper understanding of the molecular mechanism of RORα that could lead to development of therapeutics has been severely hampered by the lack of knowledge of a ligand that binds the LBD of RORα. The identification of cholesterol as ligand of the receptor RORα in accordance with the present invention, now provides new insights into the physiological role of RORα and provides RORα as a target for the screening for compounds useful for the treatment of cholesterol related-diseases. It has been shown that defects in cholesterol biosynthesis lead to a variety of clinical characteristics (Nwokoro et al., Mol Genet Metab 74:1-2 105-19 2001), covering brain damage, skeletal defects, with in some cases osteosclerosis, limb aplasia or vetebral hypoplasia. Thus, cholesterol related diseases may include endocrine disorders, atherosclerosis and cardiovascular diseases, metabolic diseases such as for instance obesity, inflammatory diseases, skin diseases, diseases related to the CNS, such as for instance Alzheimer disease and disorders in cell proliferation and apoptosis such as tumor related diseases.

In one embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of endocrine disorders, in particular disorders that are related to the synthesis of steroid hormones or the regulation of steriodogenesis. In all steroidogenic tissues, regardless of the hormones synthesized, the initial step in steroidogenic cells is the conversion of cholesterol to the first steroid, pregnenolone (Stocco, Ann Rev Physiol 63: 193-213; 2001).

In another embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of disorders of the cholesterol homeostasis. Breakdown of cholesterol homeostasis causes disease states, the most common being atherosclerosis. Hypercholesterolemia is a well-known risk factor. Using statins the present inventions shows a direct link between the activity of RORα and a potent anti-atherosclerosis molecule (Table 5) demonstrating the usefulness of RORα as molecular target for the search of compounds to fight atherosclerosis and cardiovascular diseases.

In another embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of metabolic disorders. It is known that a cascade of events initiates adipogenesis where C/EBP and PPARγ are important players. Furthermore, RORα is able to strongly induce PPARγ (Sundvold et al. Biochem. Biophys. Res. Com. 287: 383-390; 2001). SREBP promotes the adipogenic program and SREBP activity is sensitive to the level of intracellular cholesterol (Brown et al. Cell 89: 331-340,1997). Thus, in accordance with this invention, RORα is provided as a target for the screening of compounds useful for the treatment of disorders related to adipogenesis, development of obesity and insulin resistance, which can lead to type 2 diabetes. Furthermore, the mature adipocytes secrete factors that play a role in immunological responses, vascular disease and appetite regulation. Adipocytes derived factors include leptin, prostaglandin's and resistin. The present invention providing cholesterol as ligand of RORα thus provide RORα as target for screening for compounds useful for the treatment of diseases related to immune response, vascular disease and appetite regulation.

It has recently been shown that mesenchymal stem cells have the potential to differentiate into these three lineage (Pittenger et al., 1999 Science 284:143-147). Thus, an apparent reciprocal relationship is postulated to exist between the adipocyte and osteoblast phenotypes. This balance is switched toward adipocytes in osteoporotic patients. This invention provides RORα (as PPARγ or C/EBP) as important players in the adipogenesis pathway or in the differentiation of mesenchymal stem cells into adipocytic, chondrocytic or osteoblastic lineage. Thus, the present invention links RORα in this switch toward adipogenesis and therefore is a potential target for therapeutic intervention in osteoporosis.

In another embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of inflammatory diseases. Molecular links have been established between cholesterol and cytokines showing the involvement of inflammation and immunity in atherogenesis. In addition, RORα is involved in inflammation (WO01/26737, Bourdji et al. J. Biol Chem.275: 12243-12250 2000, Delerive et al., EMBO reports 21: 4248; 2001).

In another embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of skin disorders. RORα is highly expressed in skin (Becker-Andre, 1993; Biochem. Biophys. Res. Commun. 194:1371-1379). In addition, clinical observation of patients with genetic disorders of cholesterol biosynthesis report photosensitivity and patchy alopecia, as well as follicular atrophoderma.

In another embodiment, the present invention provides RORα as target for the screening of compounds useful for the treatment of Alzheimer disease. The lipoprotein allele ApoE4 is associated with an increased incidence of Alzheimer disease (Trittmatter et al. Proc. Natl. Acad. Sci.USA 90: 1977-1981; 1993); the depletion of plasma membrane cholesterol in hippocampal neurons inhibits the formation of Abeta (Simons et al. PNAS 95: 6460-6464;1998), the cleavage product of the amyloid precursor protein, that is a key factor in the pathogenesis of the disease. In addition the main characteristics of the RORα knock out mice is a severe ataxia and their cerebellum is markedly atrophied. This is implicated in rare inherited disease where people are subject to movement disorders.

EXAMPLES

Cloning and Expression of (His)₆RORα-LBD304-556

A DNA fragment encoding part of polyhedrin promoter up to the ATG codon is amplified by PCR from the pBAKPac8 plasmid (Clontech) by using the oligonucleotide RS365 (5′-ACCATCTCGCAAATAAATAAG-3′) and MG384 (5′-ATGATGATGATGATGATGGCTGCTGCCCATGGTGGGAACTCGAGGCCTGCAGGG-3′). MG384 has a 5′extension not present on the template DNA but which is encoding for a Kozak sequence in front of the ATG codon and part of the His tag which will be present in the final engineered vector. The second PCR reaction is run with the oligonucleotides MG383 (5′-GCCATCATCATCATCATCATCTGGAAGTTCTGTTCCAGGGGCCCGCAGAATTAGAACACCTTGC-3′) and MG385 (5′-GTACCAGATCTTCTAGATTCGTTACCCATCAATTTGCATTG-3′) on a plasmid template encoding the ligand binding domain (aa304 to aa 556; numbering according to SWISS-PROT P35398-1) of the RORα protein. As for the first PCR fragment, the oligonucleotide MG383 has a 5′extension complementing the extension present on the first PCR fragment and which is added by the extension of the fragment by MG384. By mixing both new fragments and with an PCR amplification with MG365 and RS365 a new fragment encoding the Kozak sequence, the ATG, the (His)₆-tag and the cleavage site for the PreScission protease cleavage site (AmershamPharmacia) is introduced in front of the RORα ligand binding domain. This new fragment has at the both end two homology regions en common with the target plasmid pBAKPac8. The integration of the engineered gene into the cloning vector is done by using the method we described earlier (Geiser et al, BioTechniques 31 88-92 ,2001). DNA sequence analysis of the resulting clones confirms that the clone is as intended. The plasmid is called pXI338.

The plasmid pXI338 is co-transfected with linearised BacPAK6 (AcNPV) virus DNA into Sf-21 insect cells using lipofection. The viral supernatant harvested after five days is subjected to plaque purification to obtain homogenous virus populations, which are subsequently amplified on small scale and analyzed for production by Western blotting. A band of correct size is readily detectable using an anti-RORα antibody (Santa Cruz, Cat.No. sc-6062) in all six analyzed cell pellets. One viral isolate is chosen for further amplification; a master virus stock, followed by a working virus stock are generated by further amplification in Sf-9 cells; titers are determined by plaque assay. A kinetic experiment reveals optimal production conditions for RORα-sLBD using 1 MOI at 1.82×106 cells/ml (TOI) for 72 hours. Under these conditions a large fraction of the protein remained soluble in the insect cells. Two Wave Bioreactor runs are performed of approx. 10-13 liters each under the above described conditions. Cells are harvested by centrifugation for 10 minutes at 6000 g in a Heraeus Cryofuge M7000, and the pellets are stored at −80° C.

Purification and Characterization of (His)₆RORα-LBD304-556

(His)₆RORα-LBD₃₀₄₋₅₅₆ is purified by Ni—NTA chromatography followed by anion-exchange and size exclusion chromatography according to standard methods. From 20-g cell paste, around 15 mg of (His)₆RORα-LBD₃₀₄₋₅₅₆ is purified. The protein runs as a monomer on the size exclusion chromatography. N-terminal sequence analysis shows that the N-terminus is blocked. Mass spectrometry analysis shows a homogeneous molecular mass of 31′515.4 corresponding to Acetyl-desMet-(His)₆RORα-LBD₃₀₄₋₅₅₆ (Acet-GSSHHHHHHLEVLFQGPAELEH . . . MQIDG). Proteolytic cleavage of the N-terminal 6×His tag by the PreScission™ protease results in a homogeneous protein that however does not yield useful crystals. In contrast, uncleaved RORα-LBD leads to crystals suitable for X-ray diffraction analysis.

Crystallization

Recombinant human RORα-LBD in 50 mM Tris-HC; pH 7.5, 100 mM NaCl, 5 MM DTT is concentrated to 14 mg/ml. Crystallization is performed using a standard vapor diffusion hanging drop set-up, with VDX crystallization plates and siliconized microscope cover slips from Hampton Research. Crystallization droplets are made by mixing on the coverslips 2.0 μl of the protein stock solution with 2.0 μl of reservoir solution and equilibrated against 700 μl of reservoir solution at 20° C. Commercially available screening kits are used to find preliminary crystallization conditions. In the refined conditions, crystals grow within 2 weeks at 20° C. to a size of 0.15×0.15×0.3 mm with a reservoir of 100 mM Tris-HCl pH 8.4, 19% PEG 6000, 0.2M CaCl₂. The space group of the native crystals is P21, with unit cell parameters a=55.9 Å, b=49.9 Å, c=60.7 Å, β=98.7° and space group P2₁. There is one monomer per asymmetric unit. The crystals diffract at the synchrotron (SNBL at ESRF, Grenoble) to at least 1.88 Å.

X-Ray Data Collection

For the native data collection, a crystal grown as described above is transferred to 5 μl of solution containing 20% glycerol (in addition to the reservoir composition) for about 10 seconds. The crystal is then rapidly mounted in a nylon CryoLoop (Hampton Research) and directly frozen in a cold nitrogen stream for X-ray data collection at 105K. Diffraction data are collected with the mar345 image plate system of the Swiss-Norwegian beaniline of the European Synchrotron Radiation Facility (λ-0.8727 Å). A total of 230 images of 1.020 rotation each are collected in time mode (15 sec per frame) with a crystal-to-detector distance of 178 mm (using a readout plate-diameter of 180 mm). Raw diffraction data are processed and scaled with the HKL program suite version 1.96.6 (Otwinowski and Minor, 1996). Crystal data and data collection statistics for the native data are shown in Table 4. The space group of the native crystals is P2₁, with unit cell parameters a=55.9 Å, b=49.9 Å, c=60.7 Å, β=98.7°. There is one monomer per asymmetric unit. The estimated B-factor by Wilson plot is 30 Å². For the Hg-derivative data collection, a crystal is soaked previously for 1 hr in 5 μl of solution containing 4 mM methylmercuric acetate (in addition to the reservoir composition). Cryocooling is then done as for the native crystal. Diffraction data are collected with the mar345 image plate system of the Swiss-Norwegian beamline of the European Synchrotron Radiation Facility (λ=0.8727 Å). A total of 287 images of 1.0° rotation each are collected in time mode (15 sec per frame) with a crystal-to-detector distance of 178 mm (using a readout plate-dimeter of 180 mm). Raw diffraction data are processed and scaled with the HKL program suite version 1.96.6 (Otwinowski and Minor, 1996). Crystal data and data collection statistics for the Hg-derivative data are shown in Table 2. The space group of the Hg-derivative crystals is P2₁, with unit cell parameters a=55.6 Å, b=50.0 Å, c=60.1 Å, β=98.0°. There is one monomer per asymmetric unit. The estimated B-factor by Wilson plot is 29 Å².

Structure Solution

Attempts to solve the structure by molecular replacement with the programs AmoRe (Navaza, 1994) or MOLREP version 6.2.5. (Vagin & Teplyakov, J.Appl.Cryst. 30, 1022-1025, 1997) by using several different models based on the coordinates of the pdb-entries 21bd (hRARγ) or 1bsx (hTRβ) are not successful. Data from a single-wavelength experiment on the mercury-substituted crystal are thus used together with a native data set for the initial phasing by SIRAS. Anomalous as well as isomorphous difference Patterson maps reveal at least one common dominant peak. SnB version 2.1 (Weeks & Miller, J.Appl.Cryst. 32, 120-124, 1999) with DREAR normalization (Blessing & Smith, J.Appl.Cryst. 32, 664-670, 1999) using the observed anomalous differences is used to determine 4 Hg-sites. The heavy-atom parameters are subsequently refined using MLPHARE version 4.1 (CCP4, 1994). Subsequent density modification with DM (CCP4, 1994) result in an excellent experimental SIRAS-map. Skeletonization with mapman enables chain-tracing and model building with O version 7.0 (Jones et al., Acta Crystallogr. A47:110-19, 1991).

Refinement

After building the protein (residues His308-Phe544 had visible electron density) and insertion of 112 water molecules into the experimental SIRAS-map, several alternate cycles of refinement and manual rebuilding result in a model with R_(cryst)=28.1% (8 Å-1.88 Å), that give excellent 2Fo-Fc and Fo-Fc maps for a ligand in the LBP. The excellent quality of the electron density allows the unambiguous identification of the ligand as being cholest-5-en-3beta-ol (cholesterol). The cholesterol ligand is then built into the electron density and X-PLOR parameter- and structure-files can be generated with the program XPLO2D (Kleywegt G., CCP4/ESF-EACBM Newsletter on Protein Crystallography 31, 45-50, 1995) that can be used to generate the X-PLOR parameter- and structure-files. Further cycles of refinement and insertion of 119 more water molecules (leading to a total of 231 water molecules) yield the final R_(cryst)=24.8% and R_(free)=26.3% (no sigma cutoff, 8 Å-1.8 Å, working set of 25592 unique reflections, test set of 1279 reflections). In general, the electron density is of excellent quality, except for the loop 493-498 which has weak density (residues 308-544 are included in model). Refinement is done with X-PLOR 3.1 (A. Bruenger, X-PLOR Version 3.1: A system for X-ray Crystallography and NMR. Yale University Press, New Haven, Conn., USA, 1992) using the Engh and Huber force field for the protein (Engh & Huber, Acta Crystallogr. A47:392-400, 1991). The chain identifiers used are A for the protein (residues His308-Phe544, numbering according to SWISS-PROT P35398-1), L for the ligand (cholesterol: residue 1) and V for the water molecules (total of 231). The atom numbers used for the ligand cholesterol in the pdb-file are not the same as the atom numbers according to IUPAC-TUB.

The quality of the model is assessed with X-PLOR 3.1 (A.Bruenger, id 1992) and PROCHECK v3.3 (Laskowski et al., J. Appl. Cryst. 1992; 26:283-91) (see Table 3). The final model of the complex RORα/cholesterol has good geometry (rms bond lengths=0.013 Å, nms bond angles=1.46°) and no residues are in disallowed regions of the Ramachandran plot, as determined by PROCHECK v3.3. Molecular graphics pictures are made with O version 7.0 (Jones et al., id 1991). TABLE 1 Number of crystals 1   Space group P2₁ Unit cell dimensions 55.9 Å, 49.9 Å, 60.7 Å β = 98.7° Number of monomers/a.u. 1   Packing coefficient 3.2 Å³/Da Resolution range 15.0-1.88 Å Number of observations 109,306    Number of rejected observations 373 (0.34%) Number of unique reflections 26,882    Wavelength 0.8727 Å Overall Data redundancy 4.1 Data completeness 99.2% <I/σ(I)> 29.5  R_(sym)(I)  0.056 Reflections with I ≧ 3σ(I) 75.1% Highest resolution shell Resolution range 1.95-1.88 Å Completeness for shell 93.2% R_(sym)(I) for shell  0.437 Reflections with I > 3σ(I) 30.5%

TABLE 2 Number of crystals 1   Space group P2₁ Unit cell dimensions 55.6 Å, 50.0 Å, 60.1 Å β = 98.0° Number of monomers/a.u. 1   Packing coefficient 3.2 Å³/Da Resolution range 10.0-1.88 Å Number of observations 121,716    Number of rejected observations 4140 (3.4%) Number of unique reflections 25,136    Wavelength 0.8727 Å Overall Data redundancy 4.8 Data completeness 93.6% < I/σ(I)> 25.3  R_(sym)(I)  0.057 Reflections with I ≧ 3σ(I) 81.8% Highest resolution shell Resolution range 1.95-1.88 Å Completeness for shell 76.2% R_(sym)(I) for shell  0.354 Reflections with I ≧ 3σ(I) 44.5% Resolution range used for phasing 10.0-1.94 Å R_(merge)(F) between native and Hg 23.8% No. of common reflections 23,396    Phasing power for acentric data  1.16 Phasing power for centric data  0.80 Overall figure of merit  0.314 R_(cullis) on centric zone  0.80 Heavy atom site 1 (x, y, z, occ, Bfac)   −0.373,   −0.546,   −0.754,   0.387, 23.9  Heavy atom site 2 (x, y, z, occ, Bfac)   −0.515,   −0.611,   −0.927,   0.429, 35.5  Heavy atom site 3 (x, y, z, occ, Bfac)   −0.839,   −0.478,   −0.700,   0.265, 29.3  Heavy atom site 4 (x, y, z, occ, Bfac)   −0.360,   −0.797,   −0.896,   0.270, 36.3 

TABLE 3 Data used in refinement resolution range 8.0-1.88 Å intensity cutoff (σ(F)) 0.0 number of reflections (working set) 25,592    number of reflections (test set) 1,279   completeness (working + test set) 99.0% Fit to data used in refinement overall R_(cryst)  0.248 overall R_(free)  0.263 Number of non-hydrogen atoms protein atoms 1,953   ligand atoms 28   water molecules 231    Mean B values mean B value for protein 38.3 Å² mean B value for ligand 20.1 Å² mean B value for water molecules 51.8 Å² Rms deviations from ideal values bond lengths 0.013 Å bond angles 1.46° dihedral angles 20.3° improper angles  1.3° Residues in disallowed region of 0   Ramachandran plot PROCHECK G-factor  0.28 Overall Structure of the RORα-LBD

The RORα-LBD adopts the canonical fold for the NR-LBDs (Wurtz et al., Nat Struct Biol 3, 206 1996) and in addition has the two helices H2* and H11*. RORα-LBD is in an agonist-bound state, as judged by the position of H12 (see also FIGS. 2 and 3). H12 in this position, together with the H3-H4 region, forms the proper interaction surface, i.e. the complete AF-2, for the coactivator (reviewed in Renaud & Moras, Cell. Mol. Life Sci., 57, 1748-1769, 2000). No coactivator peptide is added in order to obtain this crystal structure. An additional H2* helix is also found between H2 and H3 for the peroxisome proliferator-activated receptors (PPARs; Nolte et al., Nature, 395, 137-143, 1998). HI 11* is unique to RORα-LBD (and RORβ-LBD, Stehlin et al., Embo J., 20, 5822-5832, 2001) among the known LBD structures; it roughly superposes with the middle part of loop 11-12 of RAR. The overall structure of RORα-LBD is similar to the one of RORβ-LBD (e.g. as judged by FIG. 4 in Stehlin et al., id 2001), but since the coordinates of RORβ-LBD are not available, no quantitative comparison with RORα-LBD can be made. For RORα-LBD, the putaive entrance site (as judged by the solvent accessible surface of the complex) for the ligand is located between H2 and H3, and not on the H12-side, as hypothesized e.g. for RAR-γ (Renaud et al, Nature, 378, 681-689,1995). In the crystal, the RORα-LBD molecule of the asymmetric unit does not form a dimer with a neighbouring molecule. This is consistent with the finding, that on native gels RORα-LBD behaves as a monomer. The following Cys-residues have reacted with methylmercuric acetate (c.f. table 2 for fractional coordinates of Hg-sites): Cys321 (site 3), Cys429 (site 1), Cys505 (site 4) and Cys514 (site 2). These reactive Cys-residues are thus candidates for mutations into Ser, in order to possibly obtain soluble expression in E. Coli. The protein species present in the crystallization setups correspond to the following sequences His₆-tag and PreScission™ cleavage site and residue 304-556 of RORα-LBD: Ac-GSSHHHHHHLEEVLFQGPAELHLA . . . ELFTSEFEPAMQIDG

In this crystal structure, well-defined electron density is found for the subsequence residue 308-544 (numbering according to Swissprot P35398-1).

Identification of the Ligand and Description of the Ligand Binding Pocket

A small-molecule X-ray structure of 26-OH-cholesterol from the CSD (entry FIZDUN) shows a perfect, unambigous fit (after removal of the 26-OH group and rotation of 1200 around the C24-C25 bond) into this unbiased electron density. The excellent quality of the high-resolution map thus allows the identification of the ligand as being cholest-5-en-3beta-ol (cholesterol). A closer look on Ligand binding pocket of RORα shows that C27 of the terminal isopropyl-group of cholesterol makes vdW-contacts with the sidechain of Trp353, while C26 makes vdW-contacts with the sidechain of Ile360. Substituents on C26 have the potential to influence the position of H12 (e.g. bulky substituents on C26 could displace H12 from its agonist-position, thus leading to an antagonistic derivative of cholesterol). H12 in this crystal structure adopts the agonist position. It is stabilized in the agonist position by the hydrogen bond (distance 2.8 Å) between OH-Tyr540 (on H12) and NE2-His517 (on H11). These two residues are conserved among the α-, β-, and γ-isotypes of ROR.

The LBP is essentially hydrophobic on the AF-2 side (H5 N-terminus, H6, H7, H10, H12) with the exception of Tyr540 and His517 which form an intermolecular hydrogen bond (distance between OH-TyrS40 and NE2-His517 is 2.8 Å). The LBP is more polar on the H3 side (loop 1-2, H3, H5 C-terminus). The main chain NHs of Gln322 and Tyr323 on loop 1-2 and the side chains of Arg400 and Arg403 on H5 contribute to the generation of a positive electrostatic potential. A negatively charged substituent (e.g. S04-) on the 3-ol group could thus yield a derivative with considerably increased affinity (FIG. 4). There are 12 well-ordered water molecules in the hydrophilic part. 5 of these water molecules are amongst the 7 water molecules (of the total of 231 water molecules) which have the lowest B-factors (14 Å²-24 Å²). The 3-ol group of cholesterol makes, via a network of well-ordered water molecules, water-mediated hydrogen bonds to NE-Arg403, NH2-Arg403, CO-Arg400, NH1-Arg400, NH-Tyr323, OE1-Gln322 and NH-Gln322.

The average B-value for the ligand (20.1 Å²) is lower than the average B-value for the protein (38.3 Å²), consistent with the fact that excellent electron density for all non-hydrogen atoms of cholesterol is visible. Cholesterol adopts thus a well defined, single conformation in the LBP. This is in contrast with the multiple low-energy conformations described for the non-natural ligand stearic acid present in the RORβ-LBD (Stehlin et al., id 2001). The following residues have a non-hydrogen atom closer than 4 Å to the ligand cholesterol: Trp353, Cys356, Lys359, Ile360, Ala363, Val397, Arg400, Met401, Val412, Tyr413, Phe414, Phe424, Leu427, Phe432, Val436 and His517.

Design of Cholesterol Derivative Binding to LBD of RORα

Overall, there is a very good fit of the ligand cholesterol to the LBP. Nevertheless, a comparison of the vdW-surface of the ligand with the vdW-surface of the LBP shows that there are still a few possibilities for derivatizations of cholesterol (FIGS. 4 and 5), which could increase the affinity. Additional hydrogen bonds could be gained with hydroxy-groups added to position 6 (hydrogen bond via water to OE1-Glu362), position 19 (hydrogen bond to CO-Tyr413) or position 26 (hydrogen bond to OH-Tyr540 and/or NE2-His517). Considerable electrostatic interaction energy could be gained with a charged group, e.g. SO₄ ⁻, added to position 3 (hydrogen bonds and electrostatic interactions via water molecules to NH1-Arg400, NH2-Arg403, NE-Arg403, NH-Gln322 and/or to NH-Tyr323). Additional vdW-interactions could be gained by additional methyl-groups added to position 12 (vdW-contacts to the sidechains of Phe398, Met401), position 18 (vdW-contacts to the sidechains of Val412, Phe398), position 27 (vdW-contacts to the sidechains of Trp353, Cys429, Phe432) or an additional ethyl-group added to position 21 (vdW-contacts to the sidechains of Phe424, Ile433, Val436, Phe437). Modifications in positions 4 and 6 could be utilized to modify, if necessary, the physicochemical or pharmacokinetic parameters, without considerably changing the affinity. Derivatives in position 26, with a bulky substituent, would have the potential to destabilize H12 in its agonist-position, thus conferring an antagonistic activity on the derivative.

Mechanism of Action for Cholesterol

The present X-ray structure promotes the following structural mechanism of action: Cholesterol (or possibly a cholesterol-derivative) enters the LBP from the H2,H3-side, possibly guided by the electrostatic field generated from Arg400 and Arg403. The isopropyl-end of cholesterol (or a derivative in this position) then influences the other end of the LBP, which is in contact with H12, thus regulating the binding of a coactivator to the LXXLL-binding site. A cholesterol-derivative with a bulky substituent on C26 could displace H12 from its agonist conformation, thus preventing coactivator binding, while a cholesterol derivative which further stabilizes the hydrogen bond between Tyr540 and His517 would further enforce the agonist conformation.

Selected Mutations of RORα-LBD

Using the coordinates from the RORα-LBD X-ray structure a series of point mutations in the LBP are designed which should prevent binding of cholesterol and in addition a mutation is proposed which should prevent/reduce H12-stabilization via loss of the hydrogen bond between Tyr540 (on H12) and His517 (Tyr 540→Phe 540 mutation). The details of the mutations are included below. mutated Mutated clone name amino acid nucleic acids SDM1-1 Cys356 −> Leu356 TGT −> TTA SDM2-3 Ala363 −> Leu363 GCT −> CTT SDM3-4 Ala404 −> Gln404 GCC −> CAA SDM4-1 Phe432 −> Trp432 TTT −> TGG SDM5-8 His517 −> Trp517 CAT −> TGG SDM6-2 Tyr540 −> Phe540 TAC −> TTC

In a transient transfection experiment, the transcriptional activity of the RORα mutants is compared to their wild type counterpart: U2OS cells are transfected with the expression vector for RORα (ROR) or its mutated form together with a luciferase reporter gene bearing a consensus response element for RORα (RORE-tk-luc). Luciferase activity is assayed in cells from 6 well plates and related to the activity in cells transfected with the wild type RORα expression plasmid. The results are normalized to the protein content. The figure shows the mean±SD and on the left panel the results are expressed as % of induction compared to the activity of the wild type RORα. As shown in Table 4 all mutations, in the LBP (except the mutation Phe 432→Trp 432) significantly/drastically reduce the transcriptional activity of RORα leading to the conclusion that indeed RORα in its active form is bound to cholesterol. The sidechain of the mutated Trp432 has the possibility to adopt a conformation for which no steric clash with cholesterol in the LBP occurs, if the sidechains of Arg516 and Lys 520 also accordingly change their conformations. Since the latter two residues are on the surface and their sidechain conformations are not stabilised by interactions, this provides an explanation for the only slight loss of transcriptional activity for the Phe432→Trp432 mutation, in contrast to the other mutations in the LBP, for which there is no alternate side-chain conformation possible which would prevent a steric clash with cholesterol. The mutation Tyr 540 ->Phe 540 leads to a ca. 40% loss in transcriptional activity, showing that the hydrogen bond between Tyr 540 and His 517 contributes in a significant amount to the stabilization of H12 in the agonist position. TABLE 4 a.a (Swisprot P35398 −1) % Activity compared to WT 356 33.3 363 18.18 404 8.33 432 90.9 517 10 540 54.54 Effects of Fluvastation, an Inhibitor of HMG CoA-Reductase, on RORα Transcriptional Activity

Mammalian cells receive cholesterol by uptake from lipoproteins (LDL-cholesterol) and are able to synthesize cholesterol through the mevalonate pathway. In a situation where cells are cultured under conditions essentially sterol free, a key transcription factor, SREBP will be proteolytically cleaved and this releases a transcription factor to the nucleus. This transcription factor is able to transcriptionally activate HMG-CoA reductase, which is a critical step in the cholesterol biosynthesis through the mevalonate pathway. Statins, which are know drugs for hypercholesterol state are specific inhibitors of the HMG-CoA reductase. When cells are cultivated in sterol free medium, their HMG-CoA reductase is strongly activated. In this experiment cells, cultivated in medium essentially sterol free, are treated with fluvastatin. A clear decrease in RORα activity is observed, leading to the conclusion that the lowering of the intracellular cholesterol level is translated by a decrease of RORα transcriptional activity (Table 5). U2OS cells are transfected with expression vector for RORα (ROR) together with a luciferase reporter gene bearing a consensus response element for RORα (RORE-tk-luc). Luciferase activity is assayed in cells from 6 well plates and related to the activity in cells transfected with or without treatment with fluvastatin. The results are normalized to the protein content. TABLE 5 Fluvastatin Fold induction ±SEM Control 76 14 +5 μM 48 7 Control 93 6 +10 μM 38 2 Cholesterol Sulfate Inhibition of RORα Binding to RORE

Various cholesterol derivatives including cholesterol sulfate (cpd No. 12 in Table 6): are screened in essentially cholesterol-free medium for binding of RORα to the RORE. The RORα protein is expressed in the baculovirus system. The other compounds are: No. 2: 5α-Cholestan-3-one (Steraloids C4550), 3: 4-Cholesten-3α-ol (C6090), 4: 5-Cholesten-3β, 6-diol (C6418), 5: 5-Cholesten-3β, 7α-diol 7-benzoate (C6425), 6: 5-Cholesten-3β, 7β-diol 7-benzoate (C6438), 7: 5-Cholesten-3β, 19-diol (C6470), 8: 5-, 25R-Cholesten-3β, 26-diol (C6570), 9: 5-Cholesten-24β-ethyl-3β-ol acetate(C6681), 10: 5-Cholesten-3α-ol (C6730), 11: 5-Cholesten-3β-ol (C6760), 12: 5-Cholesten-3β-ol sulfate, sodium salt (C6905), 13: 7, (5α-Cholesten-3β-ol (C7400), 14: 7-Dehydrocholesterol (Fluka 30800). This indicates that cholesterol sulfate, as predicted by the X-ray structure, is able to displace cholesterol.

Effect of Cholesterol and Cholesterol Derivative on ROR Alpha Transcriptional Activity

We next establish whether in eukaryotic cells partially depleted of cholesterol, RORα transcriptional activity can be reconstituted by addition of cholesterol. We therefore treat the cells with hydroxypropyl-β-cyclodextrin (HPCD), a cyclodextrin derivative known to function as a cholesterol shuttle. HPCD treatment is used in experiments aiming at the partial depletion of intracellular cholesterol. In order to prevent an increase of intracellular cholesterol through the activation of the mevalonate pathway, cells are also treated with lovastatin while they are fed with a medium containing LDL-free serum. Using a combination of HPCD and lovastatin we find that transcription of the RORE reporter is stimulated in response to cholesterol, epicholesterol and cholestanol and to an even greater extent by cholesterol sulfate and 7-dehydrocholesterol. In contrast all the hydroxycholesterols tested do not display significant activity and the cholesterol derivative 5-cholesten-24β-ethyl-3β-ol-acetate does not trigger any increase in RORα transcriptional activity as compared to vehicle (Table 6). These data correlate well with docking studies on cholesterol derivatives using our X-ray structure of RORα. TABLE 6 Fold Compounds (10 μM) induction ±SEM Control 1 0.1 Cholesterol 3.3 0.1 Epicholesterol 2.8 0.44 Cholestanol 2.4 0.14 7-Dehydrochol 4.6 0.33 22(R)-OH-Chol 1.2 0.11 25-OH-Chol 1.6 0.06 20(S)-OH-Chol 1.2 0.11 Chol. Sulfate 5.4 0.31 27-OH-Chol 1.5 0.14 5-Cholesten-24beta 1 0.05 Ligand Exchange Screening by Mass Spectrometry

(His)₆RORα-LBD269-556 is produced in Sf9 cells and purified by Ni-NTA chromatography followed by size exclusion chromatography. The protein in Tris-HCl buffer at a concentration of 135 μM is incubated overnight at 4° C., with a 10-fold molar excess of 25-hydroxycholesterol (5-cholesten-3beta, 25-diol) or cholesterol sulfate (5-cholesten-3beta-ol-sulfate). Prior to mass spectrometry analysis, the protein is subjected to fast buffer exchange in 50 mM ammonium acetate pH 7.0 by size exclusion chromatography using disposable Centri∘Spin 20 columns (Princeton Separations, Adelphia, N.J.) according to manufacturer′s instructions. Mass spectrometry is carried out using a Q-Tof (Micromass, Manchester, UK) quadrupole time-of-flight hybrid tandem mass spectrometer equipped with a Micromass Z-type electrospray ionization source (ESI). The acquisition mass range is typically m/z 1500-4500 in 5 seconds. The mass spectrometer is tuned in order to allow detection of multiply-charged species of non-covalent complexes. The source block temperature and desolvation temperature are kept at 50° C. and 80° C., respectively. Sample cone voltage (Vc) is set to 23 volts for standard measurements. In-source induced fragmentation experiments are performed by increasing Vc up to 100 volts. The protein solution is infused at a flow rate of 10 μl/min. Data are recorded and processed using Masslynx software. Spectra are deconvoluted using MaxEnt analysis software (Micromass, Manchester, UK). The results show that both 25-OH cholesterol and cholesterol sulfate are able to fully displace cholesterol bound to the ROR-LBD. Moreover, the comparison at various cone-voltages (Vc) between the ligand/ROR-LBD-complex and the apo-ROR-LBD (without ligand) indicates that cholesterol and 25-OH cholesterol have a similar stability versus in-source collisions. In contrast, the cholesterol sulfate/ROR-LBD complex is more stable than cholesterol or 25-OH cholesterol complex.

Crystallization and X-Ray Structure of the Complex ROR(Alpha)/Cholesterol-Sulfate at 2.20 Å

Resolution: An Example of Structure Based Design

All amino acid residues relating to the complex ROR(alpha)/cholesterol-sulfate (e.g. the attached coordinates of the complex with cholesterol-sulfate, Table 9) are numbered according to splice variant Alpha-1 (i.e. P35398-2) Of SWISS-PROT entry P35398 (corresponding to the number of a given amino acid according to_SWISS-PROT P35398-1 as set out in FIG. 1 minus 33). All amino acid residues relating to the complex ROR(alpha)/cholesterol (e.g. the attached coordinates of the complex with cholesterol, Table 8) are numbered according to splice variant Alpha-2 (i.e. P35398-1) of SWISS-PROT entry P35398, except for FIGS. 7-11, where the numbering used is according to P35398-2, and except in the following discussion of the comparison with the cholesterol-sulfate complex. All amino acid residues specified in the claims are numbered according to splice variant Alpha-2 (i.e. P35398-1) of SWISS-PROT entry P35398, as set out in FIG. 1.

The proposal that cholesterol-sulfate is a ligand of ROR(alpha) is a result of structure based design, using the previously determined X-ray structure of ROR(alpha)/cholesterol at 1.63 Å resolution. In particular, the latter X-ray structure reveals that in the hydrophilic part of the LBP there is space for a substituent attached to the hydroxy-group of cholesterol, if water molecules are displaced. The presence of three arginines (Arg292, Arg370 and Arg367) and of two free backbone amide nitrogens (NH-Gln289 and NH-Tyr290) strongly suggests a negatively charged substituent with at least two hydrogen-bond acceptor functionalities (e.g. a sulfate-group). Docking studies lead to the prediction that cholesterol-sulfate should have higher affinity than cholesterol. Subsequently it is shown by MS-analysis that indeed cholesterol bound to ROR(alpha) LBD could be exchanged with cholesterol-sulfate.

The complex ROR(alpha)/cholesterol-sulfate could now be cocrystallized and the X-ray structure of the complex is solved at 2.20 Å resolution with an R_(cryst) of 19.4% and R_(free) of 21.9% for data from 20 Å to 2.20 Å. The observed binding mode shows the following features:

-   -   1). Cholesterol-sulfate and cholesterol have similar overall         modes of binding, but cholesterol-sulfate is displaced slightly         (e.g. corresponding C3-atoms by 0.85 Å) towards the hydrophilic,         positively charged, part of the LBP. This can be explained by         the optimization of electrostatic and hydrogen-bond interactions         made by the sulfate-group.     -   2.) Seven well-ordered water molecules present for cholesterol         in the hydrophilic part of the LBP have been displaced in the         complex with cholesterol-sulfate. Only one conserved water         molecule is still present which mediates interactions between         the sulfate group and NH1-Arg367 and O-Ala330.     -   3.) The sulfate group makes direct hydrogen bond interactions         with NH-Gln289, NH-Tyr290 and NH1-Arg370. This confirms the         docking hypothesis, which led to the proposal of         cholesterol-sulfate.     -   4.) The only significant changes in the protein parts of the         complexes of ROR(alpha) with cholesterol and cholesterol-sulfate         occur for the sidechain of Ile327 and the loop 1-2 (residues         Gln289 and Tyr290).         Molecular Biology, Fermentation, Purification and MS-Analysis

Generation of the construct (His)₆RORα-LBD₂₇₀₋₅₂₃, fermentation and purification are done as described above. The exchange of cholesterol by cholesterol-sulfate is done at 37° C. and confirmed by MS-analysis: Cholesterol sulfate is dissolved at 50 mM in DMSO and added at 1.0 mM final concentration to the (His)₆RORαLBD₂₇₀₋₅₂₃ solution at 73 μM. The resulting solution is incubated overnight at 37° C. and further purified by size exclusion chromatography on a SPX75 column, before concentrating to 17.6 mg/ml for crystallization trials. MS determination of the native complex is done as described previously (Kallen et al., Structure, Vol.10, 1697-1707, 2002). A control experiment is done by incubating the same amount of RORα LBD protein with 5% DMSO under identical conditions. The protein concentration is approximately 15 μM in 50 mM AcONH₄, pH 7.0. Both spectra are recorded under identical conditions with Vc=20 volts.

Crystallization

The protein used for crystallization is at 17.6 mg/ml, in 100 mM NaCl, 50 mM Tris-HCl pH7.5, 5 mM DTT. An ab inito search for crystallization conditions is undertaken. Trials are performed using a standard vapor diffusion hanging drop set-up, with VDX crystallization plates and siliconized microscope cover slips from Hampton Research. Crystallization droplets are set up at 4° C. by mixing on the coverslips 1.0 μl of the protein stock solution with 1.0 μl of a crystallization solution.

X-ray Data collection: A single crystal of approximate dimensions 60 μm×60 μm×200 μm is mounted with a nylon CryoLoop (Hampton Research) and flash-frozen in a cold nitrogen stream for X-ray data collection at 100K. Diffraction data are collected at the Swiss Light Source (operating at 300 mA), beamline X06SA, using a Marresearch CCD detector and an incident monochromatic X-ray beam with 0.9200 Å wavelength. In total, 226 images are collected with 1.0° rotation each, using an exposure time of 9 sec per frame and a crystal-to-detector distance of 150 mm. Raw diffraction data are processed and scaled with the HKL program suite version 1.96.1 (Otwinowski and Minor, 1996). The estimated B-factor by Wilson plot analysis is 32.9 Å². Crystal data and data collection statistics are shown in Table 7: Number of crystals 1   Space group P2₁ Unit cell dimensions a = 54.4 Å b = 49.9 Å c = 60.7 Å No. of monomers/a.u. 1   Packing coefficient 3.0 Å³/Da Estimated solvent content   58% Wavelength 0.9200 Å Temperature 100 K Resolution range 20.0-2.2 Å No. of observations 57,993    No. of unique reflections 16,541    Overall Resolution range 20.0-2.2 Å Data redundancy 3.5 Completeness 99.7% <I/σ(I)> 16.2  R_(merge) on intensities  0.079 Reflections with I ≧ 3σ(I) 66.4% Highest resolution shell Resolution range 2.28-2.20 Å Data redundancy 2.8 Completeness 99.4% <I/σ(I)> 1.9 R_(merge) on intensities  0.362 Reflections with I ≧ 3σ(I) 25.9%

Structure determination and refinement: The structure is determined using as starting model the coordinates of the complex ROR(alpha)/cholesterol refined to 1.63 Å resolution. The program REFMAC version 5.0 (CCP4, Acta Crystallogr. D50, 760-763, 1994) is used for refinement. Bulk solvent correction, an initial anisotropic B factor correction and restrained isotropic atomic B-factor refinement are applied. The refinement target is the maximum-likelihood target using amplitudes. No sigma cut-off is applied on the structure factor amplitudes. Cross-validation is used throughout refinement using a test set comprising 5.0% (829) of the unique reflections. Water molecules are identified with the program ARP/wARP and selected based on difference peak height (greater than 3.0σ) and distance criteria. Water molecules with temperature factors greater than 70 Å² are rejected. The program O version 7.0 (A.Jones et al., 1991) is used for model rebuilding. The refinement statistics for the final model are shown in Table 2. The final model of the complex ROR(alpha)/cholesterol-sulfate has good geometry (rms bond lengths=0.014 Å, rms bond angles=1.41°) and no residues are in a disallowed region of the Ramachandran plot.

Crystallization, data collection: The crystals used for data collection are obtained with a well solution composed of 0.2M MgCl₂, 16% w/v PEG4000, 0.1M Tris HCl, pH 8.5. The crystals reached maximal dimensions of up to 0.2 mm within 6 weeks. The complex of RORα LBD with cholesterol-sulfate is thus crystallized in a crystal form with a=54.4 Å, b=49.9 Å, c=60.7 Å, β=97.8°, P2₁ and 1 complex/asymmetric unit, which is similar to the crystal form previously obtained in the complex with cholesterol.

Conformation of cholesterol-sulfate bound to ROR(alpha) and its interactions: In general, the electron density is of excellent quality, except for amino acids 461-464 (L9-10), which has only weak density. The protein part of the refined model consists of the last two His-amino acids from the His-tag, followed by the PreScission™-site (LEVLFQG) and by amino acids 271-511 of the RORα-LBD. The refined model also contains 256 water molecules and 1 cholesterol-sulfate molecule.

The sulfate group makes direct hydrogen bond interactions with NH-Gln289 (3.0 Å), NH-Tyr290 (2.9 Å) and a bidentate interaction with NH1-Arg370 (3.0 Å, 3.1 Å). A water-mediated interaction is made with NH1-Arg367.

Comparison of the X-Ray Structures of Cholesterol-Sulfate and Cholesterol Bound to ROR(Alpha) LBD

FIG. 10 shows a superposition (using Cα's of the respective LBD's) for the ROR(alpha) complexes with cholesterol and cholesterol-sulfate. The r.m.s.d for the Cα atoms of residues Pro270-Phe511 after superposition is 0.26 Å. The only significant changes in the protein parts occur for the sidechain of Ile327 and the loop 1-2 (residues Gln289 and Tyr290): The backbone NH-atoms for Gln289 and Tyr290 move by ca. 0.8 Å towards the sulfate-group (with a concomitant movement of the respective sidechains), in order to improve the interactions with the sulfate-group. The sidechain of Ile327 has to move slightly, in order to avoid a steric clash with the terminal isopropyl-group (FIG. 9). The comparison shows that cholesterol-sulfate and cholesterol have similar overall modes of binding, but cholesterol-sulfate is displaced slightly (e.g. corresponding C3-atoms by 0.85 Å and corresponding C2-atoms by 0.7 Å) towards the hydrophilic, positively charged, part of the LBP (FIG. 9). This can be explained by the optimization of electrostatic and hydrogen-bond interactions made by the sulfate-group, group. 7 well-ordered water molecules present for cholesterol in the hydrophilic part of the LBP have been displaced in the complex with cholesterol-sulfate (FIG. 10). Only one conserved water molecule is still present which mediates interactions between the sulfate group and NH1-Arg367 and O-Ala330. The sulfate group makes direct hydrogen bond interactions with NH-Gln289, NH-Tyr290 and NH1-Arg370. This confirms the docking hypothesis, which led to the proposal of cholesterol-sulfate. TABLE 8 ATOM 1 CB HIS A 308 −3.470 26.612 −1.587 1.00 57.47 ATOM 2 CG HIS A 308 −4.960 26.750 −1.571 1.00 68.25 ATOM 3 CD2 HIS A 308 −5.766 27.800 −1.862 1.00 72.02 ATOM 4 ND1 HIS A 308 −5.794 25.720 −1.190 1.00 71.55 ATOM 5 CE1 HIS A 308 −7.049 26.131 −1.245 1.00 75.57 ATOM 6 NE2 HIS A 308 −7.061 27.389 −1.652 1.00 73.93 ATOM 7 C HIS A 308 −1.527 26.518 −0.048 1.00 46.68 ATOM 8 O HIS A 308 −1.408 25.970 1.039 1.00 46.34 ATOM 9 N HIS A 308 −2.472 28.682 −0.665 1.00 46.21 ATOM 10 CA HIS A 308 −2.791 27.256 −0.390 1.00 50.95 ATOM 11 N LEU A 309 −0.598 26.489 −0.995 1.00 43.13 ATOM 12 CA LEU A 309 0.692 25.856 −0.780 1.00 43.49 ATOM 13 CB LEU A 309 1.517 25.900 −2.069 1.00 41.03 ATOM 14 CG LEU A 309 2.967 25.402 −2.033 1.00 39.69 ATOM 15 CD1 LEU A 309 2.988 23.898 −1.765 1.00 39.26 ATOM 16 CD2 LEU A 309 3.668 25.742 −3.348 1.00 33.46 ATOM 17 C LEU A 309 1.397 26.673 0.307 1.00 41.27 ATOM 18 O LEU A 309 1.987 26.121 1.217 1.00 39.43 ATOM 19 N ALA A 310 1.371 27.994 0.158 1.00 41.63 ATOM 20 CA ALA A 310 1.972 28.894 1.125 1.00 43.60 ATOM 21 CB ALA A 310 1.772 30.334 0.692 1.00 41.23 ATOM 22 C ALA A 310 1.324 28.638 2.494 1.00 44.99 ATOM 23 O ALA A 310 2.028 28.454 3.487 1.00 42.70 ATOM 24 N GLN A 311 −0.011 28.589 2.531 1.00 46.22 ATOM 25 CA GLN A 311 −0.765 28.330 3.767 1.00 48.70 ATOM 26 CB GLN A 311 −2.266 28.239 3.472 1.00 55.01 ATOM 27 CG GLN A 311 −3.081 29.513 3.686 1.00 69.31 ATOM 28 CD GLN A 311 −4.596 29.289 3.479 1.00 78.89 ATOM 29 OE1 GLN A 311 −5.137 28.224 3.832 1.00 83.81 ATOM 30 NE2 GLN A 311 −5.275 30.278 2.876 1.00 82.00 ATOM 31 C GLN A 311 −0.339 27.015 4.413 1.00 45.78 ATOM 32 O GLN A 311 −0.043 26.949 5.599 1.00 43.47 ATOM 33 N ASN A 312 −0.332 25.966 3.604 1.00 43.80 ATOM 34 CA ASN A 312 0.023 24.624 4.049 1.00 43.06 ATOM 35 CB ASN A 312 −0.236 23.632 2.918 1.00 52.50 ATOM 36 CG ASN A 312 0.867 22.607 2.776 1.00 64.44 ATOM 37 OD1 ASN A 312 0.709 21.453 3.173 1.00 73.51 ATOM 38 ND2 ASN A 312 1.992 23.017 2.191 1.00 70.50 ATOM 39 C ASN A 312 1.437 24.436 4.606 1.00 40.68 ATOM 40 O ASN A 312 1.635 23.638 5.518 1.00 39.27 ATOM 41 N ILE A 313 2.424 25.072 3.974 1.00 39.40 ATOM 42 CA ILE A 313 3.824 24.979 4.407 1.00 38.82 ATOM 43 CB ILE A 313 4.802 25.421 3.253 1.00 34.58 ATOM 44 CG2 ILE A 313 6.169 25.806 3.799 1.00 36.01 ATOM 45 CG1 ILE A 313 4.956 24.284 2.240 1.00 37.16 ATOM 46 CD1 ILE A 313 6.005 24.537 1.154 1.00 35.61 ATOM 47 C ILE A 313 4.030 25.798 5.703 1.00 37.29 ATOM 48 O ILE A 313 4.786 25.399 6.585 1.00 39.16 ATOM 49 N SER A 314 3.298 26.906 5.823 1.00 35.32 ATOM 50 CA SER A 314 3.334 27.790 6.989 1.00 36.43 ATOM 51 CB SER A 314 2.457 29.014 6.728 1.00 37.35 ATOM 52 OG SER A 314 3.059 29.848 5.759 1.00 41.24 ATOM 53 C SER A 314 2.807 27.089 8.241 1.00 35.85 ATOM 54 O SER A 314 3.305 27.283 9.351 1.00 36.16 ATOM 55 N LYS A 315 1.777 26.288 8.033 1.00 35.61 ATOM 56 CA LYS A 315 1.131 25.547 9.094 1.00 36.35 ATOM 57 CB LYS A 315 −0.183 24.969 8.564 1.00 34.96 ATOM 58 CG LYS A 315 −1.051 24.316 9.597 1.00 38.82 ATOM 59 CD LYS A 315 −2.470 24.232 9.084 1.00 49.73 ATOM 60 CE LYS A 315 −3.386 23.556 10.082 1.00 56.14 ATOM 61 NZ LYS A 315 −3.021 22.113 10.247 1.00 65.23 ATOM 62 C LYS A 315 2.056 24.438 9.571 1.00 36.74 ATOM 63 O LYS A 315 2.102 24.130 10.757 1.00 38.14 ATOM 64 N SER A 316 2.771 23.835 8.624 1.00 35.23 ATOM 65 CA SER A 316 3.708 22.757 8.904 1.00 31.03 ATOM 66 CB SER A 316 4.268 22.189 7.591 1.00 33.89 ATOM 67 OG SER A 316 3.275 21.504 6.838 1.00 36.00 ATOM 68 C SER A 316 4.842 23.293 9.769 1.00 31.80 ATOM 69 O SER A 316 5.223 22.667 10.760 1.00 30.02 ATOM 70 N HIS A 317 5.391 24.440 9.354 1.00 29.40 ATOM 71 CA HIS A 317 6.468 25.128 10.078 1.00 31.38 ATOM 72 CB HIS A 317 6.838 26.397 9.319 1.00 28.86 ATOM 73 CG HIS A 317 7.765 27.317 10.058 1.00 30.88 ATOM 74 CD2 HIS A 317 7.590 28.583 10.506 1.00 31.39 ATOM 75 ND1 HIS A 317 9.085 27.007 10.310 1.00 31.14 ATOM 76 CE1 HIS A 317 9.686 28.042 10.866 1.00 29.44 ATOM 77 NE2 HIS A 317 8.801 29.012 10.996 1.00 30.99 ATOM 78 C HIS A 317 5.964 25.489 11.486 1.00 32.96 ATOM 79 O HIS A 317 6.647 25.271 12.491 1.00 30.21 ATOM 80 N LEU A 318 4.766 26.066 11.519 1.00 35.80 ATOM 81 CA LEU A 318 4.099 26.456 12.754 1.00 39.30 ATOM 82 CB LEU A 318 2.651 26.888 12.454 1.00 42.10 ATOM 83 CG LEU A 318 1.664 27.026 13.629 1.00 45.53 ATOM 84 CD1 LEU A 318 1.898 28.331 14.354 1.00 42.84 ATOM 85 CD2 LEU A 318 0.233 26.963 13.127 1.00 46.58 ATOM 86 C LEU A 318 4.070 25.267 13.708 1.00 39.53 ATOM 87 O LEU A 318 4.581 25.337 14.829 1.00 45.11 ATOM 88 N GLU A 319 3.517 24.157 13.235 1.00 34.75 ATOM 89 CA GLU A 319 3.378 22.951 14.040 1.00 31.78 ATOM 90 CB GLU A 319 2.258 22.088 13.464 1.00 35.64 ATOM 91 CG GLU A 319 0.966 22.887 13.304 1.00 43.85 ATOM 92 CD GLU A 319 −0.204 22.079 12.797 1.00 48.29 ATOM 93 OE1 GLU A 319 −0.046 20.870 12.496 1.00 51.24 ATOM 94 OE2 GLU A 319 −1.299 22.675 12.715 1.00 49.93 ATOM 95 C GLU A 319 4.605 22.092 14.335 1.00 31.28 ATOM 96 O GLU A 319 4.501 21.150 15.128 1.00 29.74 ATOM 97 N THR A 320 5.749 22.374 13.703 1.00 29.30 ATOM 98 CA THR A 320 6.948 21.589 13.957 1.00 25.31 ATOM 99 CB THR A 320 7.428 20.826 12.723 1.00 26.81 ATOM 100 OG1 THR A 320 7.760 21.760 11.697 1.00 31.74 ATOM 101 CG2 THR A 320 6.371 19.874 12.228 1.00 25.26 ATOM 102 C THR A 320 8.086 22.435 14.499 1.00 27.08 ATOM 103 O THR A 320 9.251 22.078 14.369 1.00 28.40 ATOM 104 N CYS A 321 7.754 23.591 15.058 1.00 27.84 ATOM 105 CA CYS A 321 8.758 24.440 15.690 1.00 32.58 ATOM 106 CB CYS A 321 8.575 25.897 15.291 1.00 35.52 ATOM 107 SG CYS A 321 9.587 26.379 13.907 1.00 31.41 ATOM 108 C CYS A 321 8.481 24.273 17.183 1.00 33.42 ATOM 109 O CYS A 321 7.315 24.272 17.584 1.00 33.09 ATOM 110 N GLN A 322 9.516 24.122 18.005 1.00 33.42 ATOM 111 CA GLN A 322 9.280 23.945 19.435 1.00 37.77 ATOM 112 CB GLN A 322 10.566 23.575 20.159 1.00 38.95 ATOM 113 CG GLN A 322 10.311 23.332 21.638 1.00 41.00 ATOM 114 CD GLN A 322 11.474 22.709 22.355 1.00 43.45 ATOM 115 OE1 GLN A 322 12.639 22.892 21.974 1.00 45.86 ATOM 116 NE2 GLN A 322 11.173 21.973 23.408 1.00 43.47 ATOM 117 C GLN A 322 8.595 25.133 20.143 1.00 38.21 ATOM 118 O GLN A 322 7.627 24.945 20.891 1.00 40.89 ATOM 119 N TYR A 323 9.087 26.348 19.893 1.00 37.01 ATOM 120 CA TYR A 323 8.518 27.545 20.513 1.00 39.53 ATOM 121 CB TYR A 323 9.576 28.318 21.306 1.00 37.75 ATOM 122 CG TYR A 323 10.245 27.509 22.370 1.00 36.25 ATOM 123 CD1 TYR A 323 11.551 27.058 22.191 1.00 40.18 ATOM 124 CE1 TYR A 323 12.185 26.279 23.139 1.00 43.63 ATOM 125 CD2 TYR A 323 9.576 27.164 23.537 1.00 38.29 ATOM 126 CE2 TYR A 323 10.196 26.386 24.500 1.00 43.87 ATOM 127 CZ TYR A 323 11.508 25.945 24.294 1.00 45.72 ATOM 128 OH TYR A 323 12.165 25.182 25.236 1.00 50.91 ATOM 129 C TYR A 323 7.916 28.496 19.502 1.00 41.39 ATOM 130 O TYR A 323 8.185 28.404 18.302 1.00 43.21 ATOM 131 N LEU A 324 7.149 29.451 20.011 1.00 38.45 ATOM 132 CA LEU A 324 6.556 30.442 19.158 1.00 36.36 ATOM 133 CB LEU A 324 5.260 30.960 19.761 1.00 40.65 ATOM 134 CG LEU A 324 4.135 29.917 19.804 1.00 47.37 ATOM 135 CD1 LEU A 324 3.021 30.333 20.790 1.00 48.02 ATOM 136 CD2 LEU A 324 3.569 29.698 18.390 1.00 48.49 ATOM 137 C LEU A 324 7.586 31.548 19.037 1.00 36.82 ATOM 138 O LEU A 324 8.369 31.791 19.955 1.00 35.71 ATOM 139 N ARG A 325 7.604 32.185 17.876 1.00 33.86 ATOM 140 CA ARG A 325 8.519 33.274 17.595 1.00 34.00 ATOM 141 CB ARG A 325 8.132 33.913 16.252 1.00 32.60 ATOM 142 CG ARG A 325 9.087 34.947 15.744 1.00 29.17 ATOM 143 CD ARG A 325 10.477 34.371 15.667 1.00 30.77 ATOM 144 NE ARG A 325 11.388 35.268 14.984 1.00 31.48 ATOM 145 CZ ARG A 325 11.340 35.518 13.681 1.00 41.33 ATOM 146 NH1 ARG A 325 10.421 34.931 12.912 1.00 39.89 ATOM 147 NH2 ARG A 325 12.195 36.383 13.147 1.00 42.61 ATOM 148 C ARG A 325 8.462 34.328 18.711 1.00 36.35 ATOM 149 O ARG A 325 9.503 34.826 19.145 1.00 37.18 ATOM 150 N GLU A 326 7.244 34.639 19.169 1.00 39.65 ATOM 151 CA GLU A 326 6.985 35.626 20.226 1.00 41.32 ATOM 152 CB GLU A 326 5.487 35.784 20.459 1.00 46.07 ATOM 153 CG GLU A 326 4.720 36.379 19.272 1.00 65.71 ATOM 154 CD GLU A 326 4.555 35.424 18.062 1.00 72.41 ATOM 155 OE1 GLU A 326 4.261 34.214 18.267 1.00 74.04 ATOM 156 OE2 GLU A 326 4.696 35.904 16.901 1.00 73.55 ATOM 157 C GLU A 326 7.659 35.211 21.520 1.00 38.16 ATOM 158 O GLU A 326 8.332 36.023 22.148 1.00 35.77 ATOM 159 N GLU A 327 7.487 33.938 21.880 1.00 35.48 ATOM 160 CA GLU A 327 8.092 33.353 23.077 1.00 38.23 ATOM 161 CB GLU A 327 7.911 31.833 23.082 1.00 46.45 ATOM 162 CG GLU A 327 6.486 31.293 23.134 1.00 57.52 ATOM 163 CD GLU A 327 6.452 29.752 23.125 1.00 63.49 ATOM 164 OE1 GLU A 327 7.441 29.113 23.557 1.00 68.14 ATOM 165 OE2 GLU A 327 5.445 29.172 22.667 1.00 68.00 ATOM 166 C GLU A 327 9.599 33.615 23.140 1.00 34.14 ATOM 167 O GLU A 327 10.098 34.218 24.076 1.00 34.19 ATOM 168 N LEU A 328 10.304 33.158 22.114 1.00 29.72 ATOM 169 CA LEU A 328 11.748 33.293 22.006 1.00 29.32 ATOM 170 CB LEU A 328 12.217 32.636 20.712 1.00 29.59 ATOM 171 CG LEU A 328 12.016 31.131 20.626 1.00 30.01 ATOM 172 CD1 LEU A 328 11.986 30.725 19.164 1.00 31.46 ATOM 173 CD2 LEU A 328 13.119 30.432 21.367 1.00 22.42 ATOM 174 C LEU A 328 12.267 34.715 22.041 1.00 28.85 ATOM 175 O LEU A 328 13.366 34.954 22.518 1.00 29.43 ATOM 176 N GLN A 329 11.486 35.654 21.520 1.00 33.80 ATOM 177 CA GLN A 329 11.901 37.056 21.481 1.00 37.54 ATOM 178 CB GLN A 329 11.093 37.808 20.439 1.00 43.64 ATOM 179 CG GLN A 329 11.132 37.198 19.050 1.00 53.22 ATOM 180 CD GLN A 329 10.283 37.983 18.065 1.00 59.04 ATOM 181 OE1 GLN A 329 9.035 37.966 18.127 1.00 59.51 ATOM 182 NE2 GLN A 329 10.953 38.720 17.174 1.00 59.14 ATOM 183 C GLN A 329 11.725 37.721 22.846 1.00 35.96 ATOM 184 O GLN A 329 12.525 38.562 23.241 1.00 30.61 ATOM 185 N GLN A 330 10.695 37.308 23.572 1.00 36.62 ATOM 186 CA GLN A 330 10.450 37.846 24.901 1.00 41.09 ATOM 187 CB GLN A 330 9.093 37.383 25.391 1.00 45.78 ATOM 188 CG GLN A 330 7.957 37.930 24.579 1.00 63.61 ATOM 189 CD GLN A 330 6.686 37.133 24.784 1.00 74.77 ATOM 190 OE1 GLN A 330 6.569 36.365 25.750 1.00 79.50 ATOM 191 NE2 GLN A 330 5.730 37.285 23.865 1.00 82.47 ATOM 192 C GLN A 330 11.515 37.477 25.951 1.00 38.55 ATOM 193 O GLN A 330 11.609 38.135 26.979 1.00 41.30 ATOM 194 N ILE A 331 12.305 36.429 25.715 1.00 32.00 ATOM 195 CA ILE A 331 13.313 36.015 26.686 1.00 23.76 ATOM 196 CB ILE A 331 13.078 34.596 27.169 1.00 22.66 ATOM 197 CG2 ILE A 331 11.656 34.435 27.630 1.00 21.34 ATOM 198 CG1 ILE A 331 13.355 33.619 26.053 1.00 24.33 ATOM 199 CD1 ILE A 331 13.364 32.235 26.555 1.00 23.84 ATOM 200 C ILE A 331 14.738 36.183 26.205 1.00 23.46 ATOM 201 O ILE A 331 15.657 35.455 26.592 1.00 27.34 ATOM 202 N THR A 332 14.918 37.180 25.354 1.00 23.06 ATOM 203 CA THR A 332 16.204 37.521 24.799 1.00 23.34 ATOM 204 CB THR A 332 15.962 38.552 23.680 1.00 31.64 ATOM 205 OG1 THR A 332 16.261 37.954 22.404 1.00 35.81 ATOM 206 CG2 THR A 332 16.735 39.863 23.912 1.00 37.99 ATOM 207 C THR A 332 17.180 38.051 25.857 1.00 20.21 ATOM 208 O THR A 332 18.401 37.887 25.749 1.00 21.02 ATOM 209 N TRP A 333 16.628 38.683 26.886 1.00 25.18 ATOM 210 CA TRP A 333 17.437 39.226 27.988 1.00 23.07 ATOM 211 CB TRP A 333 16.582 40.108 28.879 1.00 19.83 ATOM 212 CG TRP A 333 15.407 39.426 29.504 1.00 17.19 ATOM 213 CD2 TRP A 333 15.344 38.851 30.820 1.00 22.36 ATOM 214 CE2 TRP A 333 14.030 38.392 31.008 1.00 26.11 ATOM 215 CE3 TRP A 333 16.274 38.693 31.865 1.00 22.59 ATOM 216 CD1 TRP A 333 14.172 39.294 28.974 1.00 14.35 ATOM 217 NE1 TRP A 333 13.336 38.671 29.858 1.00 19.63 ATOM 218 CZ2 TRP A 333 13.607 37.778 32.213 1.00 25.43 ATOM 219 CZ3 TRP A 333 15.852 38.082 33.056 1.00 21.23 ATOM 220 CH2 TRP A 333 14.538 37.636 33.216 1.00 20.18 ATOM 221 C TRP A 333 18.028 38.116 28.826 1.00 23.38 ATOM 222 O TRP A 333 19.030 38.314 29.500 1.00 27.96 ATOM 223 N GLN A 334 17.436 36.925 28.730 1.00 24.06 ATOM 224 CA GLN A 334 17.893 35.767 29.492 1.00 22.85 ATOM 225 CB GLN A 334 16.804 34.712 29.586 1.00 22.07 ATOM 226 CG GLN A 334 15.575 35.251 30.240 1.00 25.58 ATOM 227 CD GLN A 334 14.492 34.228 30.427 1.00 29.55 ATOM 228 OE1 GLN A 334 14.621 33.066 30.029 1.00 32.54 ATOM 229 NE2 GLN A 334 13.388 34.664 31.006 1.00 31.52 ATOM 230 C GLN A 334 19.169 35.145 29.016 1.00 23.02 ATOM 231 O GLN A 334 19.180 34.020 28.519 1.00 27.49 ATOM 232 N THR A 335 20.257 35.878 29.179 1.00 21.73 ATOM 233 CA THR A 335 21.566 35.403 28.804 1.00 20.96 ATOM 234 CB THR A 335 22.436 36.595 28.396 1.00 26.82 ATOM 235 OG1 THR A 335 22.471 37.528 29.487 1.00 25.70 ATOM 236 CG2 THR A 335 21.881 37.286 27.109 1.00 18.02 ATOM 237 C THR A 335 22.237 34.647 29.978 1.00 24.27 ATOM 238 O THR A 335 21.794 34.762 31.133 1.00 25.14 ATOM 239 N PHE A 336 23.306 33.902 29.682 1.00 22.91 ATOM 240 CA PHE A 336 24.048 33.138 30.693 1.00 27.78 ATOM 241 CB PHE A 336 25.036 32.126 30.051 1.00 23.18 ATOM 242 CG PHE A 336 24.385 30.861 29.569 1.00 24.30 ATOM 243 CD1 PHE A 336 24.236 30.615 28.193 1.00 24.39 ATOM 244 CD2 PHE A 336 23.855 29.952 30.477 1.00 18.74 ATOM 245 CE1 PHE A 336 23.558 29.484 27.734 1.00 19.18 ATOM 246 CE2 PHE A 336 23.174 28.824 30.043 1.00 20.30 ATOM 247 CZ PHE A 336 23.018 28.582 28.667 1.00 24.72 ATOM 248 C PHE A 336 24.835 34.058 31.632 1.00 30.11 ATOM 249 O PHE A 336 25.560 34.953 31.182 1.00 27.94 ATOM 250 N LEU A 337 24.682 33.840 32.934 1.00 29.31 ATOM 251 CA LEU A 337 25.413 34.631 33.921 1.00 30.51 ATOM 252 CB LEU A 337 24.920 34.293 35.339 1.00 30.83 ATOM 253 CG LEU A 337 23.426 34.451 35.652 1.00 27.00 ATOM 254 CD1 LEU A 337 23.096 33.895 37.023 1.00 28.96 ATOM 255 CD2 LEU A 337 23.047 35.915 35.568 1.00 29.51 ATOM 256 C LEU A 337 26.902 34.311 33.755 1.00 30.04 ATOM 257 O LEU A 337 27.247 33.289 33.180 1.00 31.12 ATOM 258 N GLN A 338 27.779 35.200 34.226 1.00 32.35 ATOM 259 CA GLN A 338 29.231 35.036 34.098 1.00 32.95 ATOM 260 CB GLN A 338 29.954 36.189 34.782 1.00 36.81 ATOM 261 CG GLN A 338 31.330 36.423 34.214 1.00 45.74 ATOM 262 CD GLN A 338 31.292 36.625 32.691 1.00 60.39 ATOM 263 OE1 GLN A 338 30.414 37.330 32.158 1.00 62.23 ATOM 264 NE2 GLN A 338 32.237 35.995 31.985 1.00 63.44 ATOM 265 C GLN A 338 29.810 33.731 34.616 1.00 32.21 ATOM 266 O GLN A 338 30.818 33.230 34.122 1.00 31.25 ATOM 267 N GLU A 339 29.212 33.234 35.681 1.00 33.70 ATOM 268 CA GLU A 339 29.655 31.989 36.297 1.00 35.07 ATOM 269 CB GLU A 339 28.889 31.747 37.611 1.00 42.66 ATOM 270 CG GLU A 339 28.630 33.037 38.449 1.00 55.90 ATOM 271 CD GLU A 339 27.288 33.741 38.127 1.00 58.95 ATOM 272 OE1 GLU A 339 27.183 34.992 38.255 1.00 47.67 ATOM 273 OE2 GLU A 339 26.325 33.023 37.771 1.00 67.60 ATOM 274 C GLU A 339 29.340 30.878 35.319 1.00 27.81 ATOM 275 O GLU A 339 30.156 30.016 35.062 1.00 26.00 ATOM 276 N GLU A 340 28.125 30.906 34.795 1.00 26.98 ATOM 277 CA GLU A 340 27.678 29.911 33.831 1.00 28.10 ATOM 278 CB GLU A 340 26.223 30.163 33.457 1.00 29.51 ATOM 279 CG GLU A 340 25.282 30.053 34.636 1.00 26.99 ATOM 280 CD GLU A 340 23.849 30.355 34.284 1.00 30.46 ATOM 281 OE1 GLU A 340 22.970 29.488 34.510 1.00 34.56 ATOM 282 OE2 GLU A 340 23.580 31.471 33.802 1.00 31.24 ATOM 283 C GLU A 340 28.573 29.875 32.592 1.00 25.22 ATOM 284 O GLU A 340 28.910 28.798 32.096 1.00 24.52 ATOM 285 N ILE A 341 29.008 31.039 32.126 1.00 23.36 ATOM 286 CA ILE A 341 29.878 31.070 30.953 1.00 28.31 ATOM 287 CB ILE A 341 30.087 32.544 30.391 1.00 27.91 ATOM 288 CG2 ILE A 341 31.242 32.598 29.382 1.00 23.19 ATOM 289 CG1 ILE A 341 28.799 33.040 29.718 1.00 26.01 ATOM 290 CD1 ILE A 341 28.772 34.533 29.426 1.00 26.73 ATOM 291 C ILE A 341 31.210 30.382 31.208 1.00 29.36 ATOM 292 O ILE A 341 31.682 29.598 30.388 1.00 29.02 ATOM 293 N GLU A 342 31.800 30.642 32.372 1.00 36.68 ATOM 294 CA GLU A 342 33.101 30.052 32.700 1.00 37.76 ATOM 295 CB GLU A 342 33.692 30.615 34.011 1.00 50.01 ATOM 296 CG GLU A 342 32.840 30.441 35.298 1.00 68.37 ATOM 297 CD GLU A 342 32.978 29.073 36.006 1.00 77.44 ATOM 298 OE1 GLU A 342 34.115 28.691 36.384 1.00 81.72 ATOM 299 OE2 GLU A 342 31.938 28.398 36.218 1.00 79.74 ATOM 300 C GLU A 342 32.969 28.567 32.793 1.00 29.07 ATOM 301 O GLU A 342 33.873 27.835 32.421 1.00 25.34 ATOM 302 N ASN A 343 31.832 28.138 33.316 1.00 28.65 ATOM 303 CA ASN A 343 31.581 26.729 33.459 1.00 31.12 ATOM 304 CB ASN A 343 30.239 26.495 34.113 1.00 31.12 ATOM 305 CG ASN A 343 29.952 25.051 34.268 1.00 44.07 ATOM 306 OD1 ASN A 343 30.740 24.315 34.857 1.00 52.87 ATOM 307 ND2 ASN A 343 28.870 24.593 33.658 1.00 49.75 ATOM 308 C ASN A 343 31.693 26.050 32.091 1.00 31.48 ATOM 309 O ASN A 343 32.474 25.106 31.939 1.00 32.73 ATOM 310 N TYR A 344 30.980 26.578 31.089 1.00 31.34 ATOM 311 CA TYR A 344 31.056 26.028 29.720 1.00 27.38 ATOM 312 CB TYR A 344 30.133 26.778 28.747 1.00 19.95 ATOM 313 CG TYR A 344 28.678 26.486 28.906 1.00 15.00 ATOM 314 CD1 TYR A 344 27.802 27.473 29.313 1.00 12.78 ATOM 315 CE1 TYR A 344 26.453 27.216 29.464 1.00 15.93 ATOM 316 CD2 TYR A 344 28.169 25.217 28.649 1.00 16.37 ATOM 317 CE2 TYR A 344 26.805 24.939 28.802 1.00 17.65 ATOM 318 CZ TYR A 344 25.953 25.946 29.210 1.00 14.48 ATOM 319 OH TYR A 344 24.612 25.705 29.377 1.00 15.05 ATOM 320 C TYR A 344 32.467 26.132 29.189 1.00 27.55 ATOM 321 O TYR A 344 32.966 25.216 28.542 1.00 30.70 ATOM 322 N GLN A 345 33.125 27.253 29.451 1.00 28.25 ATOM 323 CA GLN A 345 34.474 27.392 28.940 1.00 31.21 ATOM 324 CB GLN A 345 34.982 28.819 29.063 1.00 29.90 ATOM 325 CG GLN A 345 34.201 29.825 28.254 1.00 35.96 ATOM 326 CD GLN A 345 34.801 31.209 28.343 1.00 40.32 ATOM 327 OE1 GLN A 345 35.654 31.469 29.187 1.00 43.48 ATOM 328 NE2 GLN A 345 34.375 32.101 27.469 1.00 40.57 ATOM 329 C GLN A 345 35.397 26.446 29.668 1.00 36.16 ATOM 330 O GLN A 345 36.485 26.128 29.179 1.00 36.49 ATOM 331 N ASN A 346 34.972 26.004 30.853 1.00 42.02 ATOM 332 CA ASN A 346 35.780 25.077 31.630 1.00 42.72 ATOM 333 CB ASN A 346 35.532 25.237 33.135 1.00 48.26 ATOM 334 CG ASN A 346 36.336 26.398 33.743 1.00 52.40 ATOM 335 OD1 ASN A 346 37.433 26.728 33.282 1.00 53.04 ATOM 336 ND2 ASN A 346 35.802 26.995 34.799 1.00 53.36 ATOM 337 C ASN A 346 35.633 23.619 31.189 1.00 40.45 ATOM 338 O ASN A 346 36.533 22.810 31.475 1.00 38.19 ATOM 339 N LYS A 347 34.559 23.293 30.449 1.00 32.64 ATOM 340 CA LYS A 347 34.351 21.912 29.980 1.00 26.11 ATOM 341 CB LYS A 347 32.985 21.742 29.338 1.00 22.43 ATOM 342 CG LYS A 347 31.860 22.141 30.218 1.00 21.17 ATOM 343 CD LYS A 347 30.533 21.903 29.569 1.00 25.53 ATOM 344 CE LYS A 347 29.436 22.235 30.550 1.00 31.64 ATOM 345 NZ LYS A 347 28.105 21.911 30.002 1.00 42.98 ATOM 346 C LYS A 347 35.417 21.514 28.979 1.00 25.51 ATOM 347 O LYS A 347 35.862 22.338 28.186 1.00 30.14 ATOM 348 N GLN A 348 35.873 20.269 29.058 1.00 23.11 ATOM 349 CA GLN A 348 36.891 19.771 28.128 1.00 29.12 ATOM 350 CB GLN A 348 37.252 18.338 28.502 1.00 37.39 ATOM 351 CG GLN A 348 37.330 18.100 30.007 1.00 50.83 ATOM 352 CD GLN A 348 38.742 17.956 30.494 1.00 55.85 ATOM 353 OE1 GLN A 348 39.428 17.011 30.122 1.00 61.65 ATOM 354 NE2 GLN A 348 39.190 18.883 31.342 1.00 65.17 ATOM 355 C GLN A 348 36.292 19.803 26.704 1.00 25.62 ATOM 356 O GLN A 348 35.067 19.729 26.570 1.00 25.40 ATOM 357 N ARG A 349 37.137 19.854 25.668 1.00 28.86 ATOM 358 CA ARG A 349 36.671 19.928 24.271 1.00 30.13 ATOM 359 CB ARG A 349 37.831 19.768 23.276 1.00 38.59 ATOM 360 CG ARG A 349 37.408 20.068 21.821 1.00 51.14 ATOM 361 CD ARG A 349 38.539 19.932 20.772 1.00 60.22 ATOM 362 NE ARG A 349 38.121 20.510 19.481 1.00 71.23 ATOM 363 CZ ARG A 349 38.525 20.126 18.263 1.00 72.91 ATOM 364 NH1 ARG A 349 39.392 19.130 18.090 1.00 72.73 ATOM 365 NH2 ARG A 349 38.041 20.753 17.198 1.00 71.22 ATOM 366 C ARG A 349 35.578 18.940 23.908 1.00 28.40 ATOM 367 O ARG A 349 34.527 19.322 23.387 1.00 26.63 ATOM 368 N GLU A 350 35.857 17.662 24.165 1.00 29.38 ATOM 369 CA GLU A 350 34.932 16.565 23.877 1.00 27.83 ATOM 370 CB GLU A 350 35.586 15.215 24.184 1.00 33.12 ATOM 371 CG GLU A 350 35.794 14.956 25.684 1.00 35.99 ATOM 372 CD GLU A 350 37.212 15.247 26.148 1.00 38.01 ATOM 373 OE1 GLU A 350 37.736 14.408 26.913 1.00 43.71 ATOM 374 OE2 GLU A 350 37.809 16.283 25.756 1.00 32.70 ATOM 375 C GLU A 350 33.640 16.687 24.654 1.00 24.52 ATOM 376 O GLU A 350 32.596 16.237 24.195 1.00 25.09 ATOM 377 N VAL A 351 33.709 17.268 25.847 1.00 22.09 ATOM 378 CA VAL A 351 32.513 17.457 26.645 1.00 20.23 ATOM 379 CB VAL A 351 32.854 17.885 28.107 1.00 20.75 ATOM 380 CG1 VAL A 351 31.583 18.062 28.911 1.00 19.11 ATOM 381 CG2 VAL A 351 33.778 16.851 28.759 1.00 24.36 ATOM 382 C VAL A 351 31.625 18.521 25.990 1.00 20.47 ATOM 383 O VAL A 351 30.405 18.343 25.878 1.00 21.64 ATOM 384 N MET A 352 32.211 19.646 25.592 1.00 23.84 ATOM 385 CA MET A 352 31.414 20.705 24.952 1.00 23.93 ATOM 386 CB MET A 352 32.235 22.008 24.824 1.00 28.98 ATOM 387 CG MET A 352 31.437 23.318 24.552 1.00 26.03 ATOM 388 SD MET A 352 30.054 23.586 25.661 1.00 27.59 ATOM 389 CE MET A 352 29.087 24.826 24.802 1.00 28.37 ATOM 390 C MET A 352 30.897 20.191 23.580 1.00 21.58 ATOM 391 O MET A 352 29.743 20.392 23.241 1.00 23.25 ATOM 392 N TRP A 353 31.714 19.450 22.847 1.00 20.93 ATOM 393 CA TRP A 353 31.249 18.904 21.567 1.00 22.11 ATOM 394 CB TRP A 353 32.375 18.137 20.884 1.00 23.30 ATOM 395 CG TRP A 353 33.205 18.935 19.922 1.00 29.85 ATOM 396 CD2 TRP A 353 33.052 18.969 18.489 1.00 29.97 ATOM 397 CE2 TRP A 353 34.093 19.776 17.974 1.00 30.39 ATOM 398 CE3 TRP A 353 32.135 18.385 17.592 1.00 30.52 ATOM 399 CD1 TRP A 353 34.298 19.711 20.209 1.00 30.84 ATOM 400 NE1 TRP A 353 34.838 20.216 19.038 1.00 32.97 ATOM 401 CZ2 TRP A 353 34.248 20.015 16.599 1.00 32.23 ATOM 402 CZ3 TRP A 353 32.291 18.623 16.228 1.00 29.92 ATOM 403 CH2 TRP A 353 33.344 19.432 15.748 1.00 30.15 ATOM 404 C TRP A 353 30.022 17.992 21.733 1.00 19.54 ATOM 405 O TRP A 353 29.027 18.132 21.014 1.00 21.17 ATOM 406 N GLN A 354 30.059 17.088 22.714 1.00 20.89 ATOM 407 CA GLN A 354 28.938 16.158 22.939 1.00 19.30 ATOM 408 CB GLN A 354 29.263 15.167 24.077 1.00 23.50 ATOM 409 CG GLN A 354 28.393 13.888 24.093 1.00 24.75 ATOM 410 CD GLN A 354 27.436 13.788 25.282 1.00 23.74 ATOM 411 OE1 GLN A 354 27.297 14.737 26.049 1.00 29.52 ATOM 412 NE2 GLN A 354 26.767 12.629 25.427 1.00 20.53 ATOM 413 C GLN A 354 27.647 16.875 23.248 1.00 16.93 ATOM 414 O GLN A 354 26.566 16.516 22.759 1.00 16.41 ATOM 415 N LEU A 355 27.747 17.885 24.098 1.00 19.29 ATOM 416 CA LEU A 355 26.574 18.645 24.468 1.00 15.90 ATOM 417 CB LEU A 355 26.913 19.657 25.579 1.00 15.22 ATOM 418 CG LEU A 355 25.802 20.622 25.993 1.00 17.93 ATOM 419 CD1 LEU A 355 24.582 19.962 26.610 1.00 14.68 ATOM 420 CD2 LEU A 355 26.418 21.667 26.918 1.00 21.31 ATOM 421 C LEU A 355 25.993 19.357 23.240 1.00 11.91 ATOM 422 O LEU A 355 24.790 19.348 23.054 1.00 14.23 ATOM 423 N CYS A 356 26.827 20.005 22.441 1.00 16.77 ATOM 424 CA CYS A 356 26.307 20.691 21.244 1.00 22.19 ATOM 425 CB CYS A 356 27.436 21.450 20.561 1.00 21.05 ATOM 426 SG CYS A 356 28.067 22.797 21.523 1.00 23.18 ATOM 427 C CYS A 356 25.640 19.676 20.263 1.00 21.08 ATOM 428 O CYS A 356 24.584 19.943 19.679 1.00 22.08 ATOM 429 N ALA A 357 26.228 18.483 20.160 1.00 22.51 ATOM 430 CA ALA A 357 25.678 17.449 19.304 1.00 19.05 ATOM 431 CB ALA A 357 26.606 16.267 19.264 1.00 25.06 ATOM 432 C ALA A 357 24.296 17.048 19.778 1.00 20.99 ATOM 433 O ALA A 357 23.387 16.919 18.975 1.00 21.56 ATOM 434 N ILE A 358 24.104 16.887 21.092 1.00 21.52 ATOM 435 CA ILE A 358 22.782 16.522 21.627 1.00 19.00 ATOM 436 CB ILE A 358 22.812 16.382 23.202 1.00 19.36 ATOM 437 CG2 ILE A 358 21.374 16.383 23.779 1.00 15.59 ATOM 438 CG1 ILE A 358 23.623 15.153 23.614 1.00 22.16 ATOM 439 CD1 ILE A 358 24.073 15.174 25.079 1.00 23.75 ATOM 440 C ILE A 358 21.747 17.597 21.291 1.00 18.17 ATOM 441 O ILE A 358 20.590 17.322 20.947 1.00 17.46 ATOM 442 N LYS A 359 22.171 18.843 21.443 1.00 22.77 ATOM 443 CA LYS A 359 21.291 19.983 21.206 1.00 21.40 ATOM 444 CB LYS A 359 21.931 21.234 21.809 1.00 23.15 ATOM 445 CG LYS A 359 22.175 21.133 23.334 1.00 24.28 ATOM 446 CD LYS A 359 20.879 20.855 24.063 1.00 24.08 ATOM 447 CE LYS A 359 21.061 20.872 25.562 1.00 31.76 ATOM 448 NZ LYS A 359 19.730 20.695 26.175 1.00 29.13 ATOM 449 C LYS A 359 20.925 20.166 19.721 1.00 16.10 ATOM 450 O LYS A 359 19.764 20.377 19.403 1.00 20.28 ATOM 451 N ILE A 360 21.914 20.094 18.841 1.00 15.62 ATOM 452 CA ILE A 360 21.666 20.199 17.402 1.00 18.38 ATOM 453 CB ILE A 360 22.959 19.988 16.595 1.00 24.95 ATOM 454 CG2 ILE A 360 22.659 19.672 15.136 1.00 28.87 ATOM 455 CG1 ILE A 360 23.846 21.221 16.659 1.00 25.71 ATOM 456 CD1 ILE A 360 25.260 20.940 16.214 1.00 28.76 ATOM 457 C ILE A 360 20.707 19.085 17.026 1.00 16.86 ATOM 458 O ILE A 360 19.678 19.341 16.433 1.00 23.45 ATOM 459 N THR A 361 20.986 17.861 17.467 1.00 17.32 ATOM 460 CA THR A 361 20.131 16.724 17.118 1.00 17.15 ATOM 461 CB THR A 361 20.647 15.411 17.703 1.00 21.09 ATOM 462 OG1 THR A 361 22.030 15.263 17.385 1.00 21.21 ATOM 463 CG2 THR A 361 19.842 14.207 17.146 1.00 23.13 ATOM 464 C THR A 361 18.687 16.887 17.514 1.00 22.12 ATOM 465 O THR A 361 17.786 16.414 16.813 1.00 22.98 ATOM 466 N GLU A 362 18.455 17.530 18.660 1.00 22.63 ATOM 467 CA GLU A 362 17.092 17.761 19.121 1.00 21.83 ATOM 468 CB GLU A 362 17.076 18.335 20.541 1.00 25.44 ATOM 469 CG GLU A 362 15.729 18.156 21.228 1.00 45.77 ATOM 470 CD GLU A 362 15.382 19.260 22.253 1.00 61.04 ATOM 471 OE1 GLU A 362 16.281 19.648 23.059 1.00 67.71 ATOM 472 OE2 GLU A 362 14.199 19.723 22.249 1.00 58.48 ATOM 473 C GLU A 362 16.407 18.717 18.137 1.00 17.52 ATOM 474 O GLU A 362 15.226 18.567 17.836 1.00 18.31 ATOM 475 N ALA A 363 17.148 19.711 17.656 1.00 17.89 ATOM 476 CA ALA A 363 16.613 20.652 16.656 1.00 22.83 ATOM 477 CB ALA A 363 17.624 21.753 16.358 1.00 21.95 ATOM 478 C ALA A 363 16.304 19.896 15.348 1.00 21.89 ATOM 479 O ALA A 363 15.286 20.140 14.706 1.00 24.25 ATOM 480 N ILE A 364 17.196 18.994 14.952 1.00 23.12 ATOM 481 CA ILE A 364 16.995 18.214 13.715 1.00 23.74 ATOM 482 CB ILE A 364 18.255 17.379 13.357 1.00 20.60 ATOM 483 CG2 ILE A 364 17.943 16.320 12.288 1.00 20.36 ATOM 484 CG1 ILE A 364 19.349 18.329 12.855 1.00 16.57 ATOM 485 CD1 ILE A 364 20.748 17.766 12.820 1.00 17.77 ATOM 486 C ILE A 364 15.709 17.382 13.705 1.00 28.19 ATOM 487 O ILE A 364 14.969 17.380 12.715 1.00 29.54 ATOM 488 N GLN A 365 15.370 16.784 14.842 1.00 28.50 ATOM 489 CA GLN A 365 14.159 15.976 14.937 1.00 28.61 ATOM 490 CB GLN A 365 14.049 15.352 16.309 1.00 34.56 ATOM 491 CG GLN A 365 15.324 14.645 16.719 1.00 46.55 ATOM 492 CD GLN A 365 15.071 13.640 17.800 1.00 53.78 ATOM 493 OE1 GLN A 365 13.968 13.106 17.901 1.00 64.74 ATOM 494 NE2 GLN A 365 16.077 13.366 18.617 1.00 55.00 ATOM 495 C GLN A 365 12.893 16.737 14.620 1.00 26.94 ATOM 496 O GLN A 365 11.919 16.145 14.172 1.00 30.81 ATOM 497 N TYR A 366 12.884 18.036 14.903 1.00 26.99 ATOM 498 CA TYR A 366 11.733 18.889 14.598 1.00 23.20 ATOM 499 CB TYR A 366 11.822 20.212 15.376 1.00 25.77 ATOM 500 CG TYR A 366 11.345 20.112 16.816 1.00 27.13 ATOM 501 CD1 TYR A 366 12.246 20.050 17.880 1.00 27.24 ATOM 502 CE1 TYR A 366 11.787 19.956 19.198 1.00 32.73 ATOM 503 CD2 TYR A 366 9.984 20.075 17.103 1.00 29.26 ATOM 504 CE2 TYR A 366 9.521 19.976 18.402 1.00 33.96 ATOM 505 CZ TYR A 366 10.420 19.917 19.445 1.00 36.94 ATOM 506 OH TYR A 366 9.925 19.808 20.729 1.00 45.77 ATOM 507 C TYR A 366 11.743 19.165 13.084 1.00 22.71 ATOM 508 O TYR A 366 10.688 19.258 12.450 1.00 21.29 ATOM 509 N VAL A 367 12.948 19.314 12.527 1.00 23.15 ATOM 510 CA VAL A 367 13.130 19.536 11.085 1.00 25.23 ATOM 511 CB VAL A 367 14.586 19.907 10.742 1.00 22.53 ATOM 512 CG1 VAL A 367 14.798 19.914 9.224 1.00 20.69 ATOM 513 CG2 VAL A 367 14.878 21.280 11.292 1.00 17.32 ATOM 514 C VAL A 367 12.650 18.303 10.281 1.00 28.13 ATOM 515 O VAL A 367 12.027 18.449 9.236 1.00 28.63 ATOM 516 N VAL A 368 12.929 17.098 10.771 1.00 27.16 ATOM 517 CA VAL A 368 12.450 15.890 10.116 1.00 27.59 ATOM 518 CB VAL A 368 13.048 14.606 10.759 1.00 23.81 ATOM 519 CG1 VAL A 368 12.340 13.380 10.226 1.00 29.32 ATOM 520 CG2 VAL A 368 14.550 14.505 10.469 1.00 18.99 ATOM 521 C VAL A 368 10.894 15.861 10.144 1.00 32.37 ATOM 522 O VAL A 368 10.268 15.429 9.159 1.00 33.74 ATOM 523 N GLU A 369 10.268 16.324 11.242 1.00 26.37 ATOM 524 CA GLU A 369 8.801 16.364 11.318 1.00 26.23 ATOM 525 CB GLU A 369 8.281 16.756 12.712 1.00 29.58 ATOM 526 CG GLU A 369 8.304 15.647 13.763 1.00 33.78 ATOM 527 CD GLU A 369 7.736 14.303 13.284 1.00 34.63 ATOM 528 OE1 GLU A 369 6.610 14.253 12.741 1.00 36.64 ATOM 529 OE2 GLU A 369 8.430 13.280 13.476 1.00 40.81 ATOM 530 C GLU A 369 8.269 17.358 10.291 1.00 26.20 ATOM 531 O GLU A 369 7.213 17.143 9.713 1.00 29.54 ATOM 532 N PHE A 370 8.970 18.476 10.118 1.00 24.75 ATOM 533 CA PHE A 370 8.607 19.475 9.114 1.00 24.70 ATOM 534 CB PHE A 370 9.615 20.615 9.162 1.00 23.84 ATOM 535 CG PHE A 370 9.415 21.663 8.093 1.00 24.23 ATOM 536 CD1 PHE A 370 8.265 22.444 8.071 1.00 24.20 ATOM 537 CD2 PHE A 370 10.415 21.918 7.161 1.00 24.12 ATOM 538 CE1 PHE A 370 8.120 23.468 7.150 1.00 27.38 ATOM 539 CE2 PHE A 370 10.276 22.943 6.234 1.00 26.73 ATOM 540 CZ PHE A 370 9.125 23.722 6.231 1.00 24.57 ATOM 541 C PHE A 370 8.648 18.805 7.712 1.00 26.16 ATOM 542 O PHE A 370 7.666 18.841 6.966 1.00 24.95 ATOM 543 N ALA A 371 9.780 18.172 7.395 1.00 25.24 ATOM 544 CA ALA A 371 9.988 17.459 6.130 1.00 31.38 ATOM 545 CB ALA A 371 11.281 16.681 6.171 1.00 27.13 ATOM 546 C ALA A 371 8.829 16.525 5.794 1.00 33.49 ATOM 547 O ALA A 371 8.328 16.550 4.674 1.00 35.75 ATOM 548 N LYS A 372 8.380 15.730 6.766 1.00 32.11 ATOM 549 CA LYS A 372 7.260 14.817 6.547 1.00 32.07 ATOM 550 CB LYS A 372 7.025 13.969 7.780 1.00 31.18 ATOM 551 CG LYS A 372 8.142 13.030 8.132 1.00 34.27 ATOM 552 CD LYS A 372 7.714 12.198 9.322 1.00 41.43 ATOM 553 CE LYS A 372 8.898 11.535 9.996 1.00 47.18 ATOM 554 NZ LYS A 372 8.490 10.731 11.203 1.00 52.21 ATOM 555 C LYS A 372 5.920 15.464 6.175 1.00 36.43 ATOM 556 O LYS A 372 5.047 14.804 5.612 1.00 39.27 ATOM 557 N ARG A 373 5.742 16.735 6.511 1.00 38.37 ATOM 558 CA ARG A 373 4.484 17.435 6.242 1.00 40.66 ATOM 559 CB ARG A 373 4.201 18.447 7.355 1.00 45.55 ATOM 560 CG ARG A 373 4.681 18.002 8.714 1.00 54.93 ATOM 561 CD ARG A 373 3.682 17.131 9.441 1.00 59.22 ATOM 562 NE ARG A 373 2.817 17.960 10.278 1.00 65.72 ATOM 563 CZ ARG A 373 2.860 17.988 11.607 1.00 63.53 ATOM 564 NH1 ARG A 373 3.723 17.222 12.261 1.00 61.86 ATOM 565 NH2 ARG A 373 2.057 18.802 12.281 1.00 66.65 ATOM 566 C ARG A 373 4.503 18.179 4.916 1.00 41.35 ATOM 567 O ARG A 373 3.496 18.773 4.516 1.00 40.31 ATOM 568 N ILE A 374 5.669 18.203 4.271 1.00 41.14 ATOM 569 CA ILE A 374 5.806 18.883 2.996 1.00 40.72 ATOM 570 CB ILE A 374 7.237 19.329 2.697 1.00 36.14 ATOM 571 CG2 ILE A 374 7.298 19.939 1.299 1.00 32.36 ATOM 572 CG1 ILE A 374 7.675 20.387 3.702 1.00 34.12 ATOM 573 CD1 ILE A 374 9.159 20.603 3.712 1.00 36.75 ATOM 574 C ILE A 374 5.302 18.054 1.831 1.00 45.90 ATOM 575 O ILE A 374 5.733 16.929 1.583 1.00 42.19 ATOM 576 N ASP A 375 4.301 18.625 1.183 1.00 50.81 ATOM 577 CA ASP A 375 3.654 18.084 −0.002 1.00 52.36 ATOM 578 CB ASP A 375 2.859 19.229 −0.649 1.00 60.93 ATOM 579 CG ASP A 375 3.543 20.613 −0.449 1.00 68.87 ATOM 580 OD1 ASP A 375 4.421 20.987 −1.277 1.00 67.94 ATOM 581 OD2 ASP A 375 3.225 21.301 0.561 1.00 63.03 ATOM 582 C ASP A 375 4.690 17.547 −0.998 1.00 48.88 ATOM 583 O ASP A 375 5.454 18.309 −1.595 1.00 48.00 ATOM 584 N GLY A 376 4.743 16.234 −1.152 1.00 45.67 ATOM 585 CA GLY A 376 5.683 15.669 −2.103 1.00 43.48 ATOM 586 C GLY A 376 6.816 14.872 −1.514 1.00 40.36 ATOM 587 O GLY A 376 7.200 13.837 −2.052 1.00 38.28 ATOM 588 N PHE A 377 7.339 15.346 −0.394 1.00 37.97 ATOM 589 CA PHE A 377 8.448 14.677 0.270 1.00 34.67 ATOM 590 CB PHE A 377 8.826 15.430 1.567 1.00 34.08 ATOM 591 CG PHE A 377 10.054 14.887 2.245 1.00 29.16 ATOM 592 CD1 PHE A 377 11.305 15.422 1.962 1.00 27.28 ATOM 593 CD2 PHE A 377 9.964 13.778 3.096 1.00 30.07 ATOM 594 CE1 PHE A 377 12.453 14.859 2.496 1.00 28.02 ATOM 595 CE2 PHE A 377 11.095 13.205 3.637 1.00 29.05 ATOM 596 CZ PHE A 377 12.353 13.746 3.333 1.00 28.74 ATOM 597 C PHE A 377 8.203 13.197 0.572 1.00 34.90 ATOM 598 O PHE A 377 9.076 12.361 0.305 1.00 35.66 ATOM 599 N MET A 378 7.060 12.871 1.169 1.00 34.38 ATOM 600 CA MET A 378 6.766 11.491 1.512 1.00 38.67 ATOM 601 CB MET A 378 5.565 11.393 2.457 1.00 41.83 ATOM 602 CG MET A 378 5.882 11.754 3.909 1.00 48.90 ATOM 603 SD MET A 378 7.422 10.982 4.496 1.00 56.77 ATOM 604 CE MET A 378 6.884 9.291 4.787 1.00 57.67 ATOM 605 C MET A 378 6.574 10.586 0.301 1.00 42.95 ATOM 606 O MET A 378 6.564 9.363 0.428 1.00 43.36 ATOM 607 N GLU A 379 6.427 11.184 −0.877 1.00 44.95 ATOM 608 CA GLU A 379 6.248 10.399 −2.086 1.00 45.80 ATOM 609 CB GLU A 379 5.359 11.144 −3.071 1.00 52.39 ATOM 610 CG GLU A 379 3.943 11.354 −2.587 1.00 61.32 ATOM 611 CD GLU A 379 3.127 12.219 −3.537 1.00 71.44 ATOM 612 OE1 GLU A 379 3.681 13.182 −4.126 1.00 73.32 ATOM 613 OE2 GLU A 379 1.920 11.933 −3.693 1.00 77.96 ATOM 614 C GLU A 379 7.581 10.057 −2.741 1.00 43.64 ATOM 615 O GLU A 379 7.655 9.144 −3.553 1.00 43.83 ATOM 616 N LEU A 380 8.633 10.794 −2.409 1.00 40.33 ATOM 617 CA LEU A 380 9.939 10.521 −2.986 1.00 40.49 ATOM 618 CB LEU A 380 10.949 11.562 −2.536 1.00 39.57 ATOM 619 CG LEU A 380 10.996 12.909 −3.242 1.00 43.35 ATOM 620 CD1 LEU A 380 9.660 13.313 −3.786 1.00 48.51 ATOM 621 CD2 LEU A 380 11.496 13.947 −2.266 1.00 43.53 ATOM 622 C LEU A 380 10.374 9.151 −2.509 1.00 43.17 ATOM 623 O LEU A 380 9.702 8.546 −1.675 1.00 41.79 ATOM 624 N CYS A 381 11.480 8.650 −3.053 1.00 46.89 ATOM 625 CA CYS A 381 11.988 7.339 −2.651 1.00 51.11 ATOM 626 CB CYS A 351 12.676 6.632 −3.838 1.00 48.63 ATOM 627 SG CYS A 381 14.146 7.457 −4.487 1.00 48.71 ATOM 628 C CYS A 381 12.938 7.479 −1.437 1.00 53.70 ATOM 629 O CYS A 381 13.731 8.427 −1.357 1.00 54.89 ATOM 630 N GLN A 382 12.813 6.559 −0.478 1.00 56.40 ATOM 631 CA GLN A 382 13.625 6.552 0.747 1.00 57.37 ATOM 632 CB GLN A 382 13.717 5.125 1.299 1.00 66.42 ATOM 633 CG GLN A 382 14.527 4.981 2.596 1.00 80.23 ATOM 634 CD GLN A 382 14.924 3.529 2.908 1.00 87.56 ATOM 635 OE1 GLN A 382 14.364 2.579 2.351 1.00 93.99 ATOM 636 NE2 GLN A 382 15.916 3.361 3.781 1.00 90.30 ATOM 637 C GLN A 382 15.030 7.108 0.529 1.00 52.28 ATOM 638 O GLN A 382 15.534 7.891 1.315 1.00 52.44 ATOM 639 N ASN A 383 15.644 6.716 −0.571 1.00 48.24 ATOM 640 CA ASN A 383 16.975 7.166 −0.891 1.00 46.79 ATOM 641 CB ASN A 383 17.393 6.604 −2.241 1.00 55.14 ATOM 642 CG ASN A 383 17.496 5.100 −2.232 1.00 63.92 ATOM 643 OD1 ASN A 383 18.603 4.559 −2.272 1.00 68.19 ATOM 644 ND2 ASN A 383 16.350 4.405 −2.198 1.00 65.25 ATOM 645 C ASN A 383 17.000 8.669 −0.986 1.00 42.13 ATOM 646 O ASN A 383 17.853 9.331 −0.408 1.00 38.96 ATOM 647 N ASP A 384 16.064 9.203 −1.749 1.00 35.42 ATOM 648 CA ASP A 384 16.015 10.633 −1.945 1.00 35.36 ATOM 649 CB ASP A 384 15.137 10.984 −3.146 1.00 35.18 ATOM 650 CG ASP A 384 15.790 10.618 −4.491 1.00 36.49 ATOM 651 OD1 ASP A 384 16.835 9.919 −4.525 1.00 35.12 ATOM 652 OD2 ASP A 384 15.245 11.049 −5.519 1.00 34.59 ATOM 653 C ASP A 384 15.578 11.376 −0.701 1.00 30.33 ATOM 654 O ASP A 384 15.999 12.501 −0.484 1.00 27.59 ATOM 655 N GLN A 385 14.713 10.760 0.098 1.00 31.50 ATOM 656 CA GLN A 385 14.280 11.403 1.348 1.00 33.11 ATOM 657 CB GLN A 385 13.215 10.577 2.033 1.00 28.85 ATOM 658 CG GLN A 385 11.932 10.516 1.281 1.00 29.25 ATOM 659 CD GLN A 385 10.981 9.578 1.942 1.00 35.13 ATOM 660 OE1 GLN A 385 11.392 8.704 2.711 1.00 39.80 ATOM 661 NE2 GLN A 385 9.703 9.737 1.663 1.00 34.78 ATOM 662 C GLN A 385 15.488 11.552 2.277 1.00 31.53 ATOM 663 O GLN A 385 15.751 12.632 2.816 1.00 29.68 ATOM 664 N ILE A 386 16.251 10.466 2.394 1.00 29.20 ATOM 665 CA ILE A 386 17.452 10.430 3.208 1.00 31.16 ATOM 666 CB ILE A 386 17.992 8.987 3.310 1.00 30.97 ATOM 667 CG2 ILE A 386 19.411 8.959 3.925 1.00 29.51 ATOM 668 CG1 ILE A 386 16.982 8.148 4.103 1.00 31.82 ATOM 669 CD1 ILE A 386 17.452 6.761 4.458 1.00 39.13 ATOM 670 C ILE A 386 18.518 11.411 2.696 1.00 30.95 ATOM 671 O ILE A 386 19.068 12.189 3.473 1.00 31.12 ATOM 672 N VAL A 387 18.788 11.400 1.392 1.00 30.52 ATOM 673 CA VAL A 387 19.771 12.314 0.800 1.00 26.90 ATOM 674 CB VAL A 387 19.877 12.122 −0.763 1.00 25.37 ATOM 675 CG1 VAL A 387 20.555 13.328 −1.412 1.00 20.02 ATOM 676 CG2 VAL A 387 20.658 10.864 −1.088 1.00 22.89 ATOM 677 C VAL A 387 19.394 13.786 1.104 1.00 28.03 ATOM 678 O VAL A 387 20.265 14.602 1.446 1.00 27.40 ATOM 679 N LEU A 388 18.099 14.114 0.975 1.00 27.01 ATOM 680 CA LEU A 388 17.606 15.482 1.212 1.00 25.83 ATOM 681 CB LEU A 388 16.149 15.631 0.776 1.00 25.27 ATOM 682 CG LEU A 388 15.822 15.597 −0.723 1.00 23.66 ATOM 683 CD1 LEU A 388 14.344 15.786 −0.898 1.00 24.29 ATOM 684 CD2 LEU A 388 16.587 16.686 −1.461 1.00 27.16 ATOM 685 C LEU A 388 17.738 15.871 2.683 1.00 26.40 ATOM 686 O LEU A 388 18.094 16.998 2.998 1.00 25.91 ATOM 687 N LEU A 389 17.461 14.928 3.572 1.00 25.45 ATOM 688 CA LEU A 389 17.578 15.192 4.994 1.00 23.81 ATOM 689 CB LEU A 389 16.915 14.096 5.803 1.00 23.38 ATOM 690 CG LEU A 389 15.402 14.206 5.789 1.00 22.32 ATOM 691 CD1 LEU A 389 14.785 13.003 6.476 1.00 25.13 ATOM 692 CD2 LEU A 389 14.984 15.501 6.427 1.00 19.09 ATOM 693 C LEU A 389 19.020 15.299 5.376 1.00 21.15 ATOM 694 O LEU A 389 19.410 16.257 6.028 1.00 26.81 ATOM 695 N LYS A 390 19.849 14.373 4.916 1.00 18.69 ATOM 696 CA LYS A 390 21.250 14.429 5.273 1.00 21.34 ATOM 697 CB LYS A 390 22.050 13.326 4.592 1.00 24.41 ATOM 698 CG LYS A 390 21.938 11.960 5.200 1.00 29.06 ATOM 699 CD LYS A 390 23.067 11.081 4.673 1.00 31.45 ATOM 700 CE LYS A 390 23.062 9.718 5.342 1.00 40.63 ATOM 701 NZ LYS A 390 24.240 8.890 4.933 1.00 46.61 ATOM 702 C LYS A 390 21.884 15.751 4.907 1.00 25.73 ATOM 703 O LYS A 390 22.706 16.287 5.644 1.00 26.32 ATOM 704 N ALA A 391 21.478 16.295 3.770 1.00 25.48 ATOM 705 CA ALA A 391 22.065 17.527 3.281 1.00 23.46 ATOM 706 CB ALA A 391 22.076 17.505 1.766 1.00 26.48 ATOM 707 C ALA A 391 21.401 18.795 3.750 1.00 20.95 ATOM 708 O ALA A 391 22.074 19.789 4.005 1.00 27.25 ATOM 709 N GLY A 392 20.082 18.773 3.838 1.00 21.07 ATOM 710 CA GLY A 392 19.349 19.965 4.202 1.00 22.76 ATOM 711 C GLY A 392 18.923 20.133 5.638 1.00 23.17 ATOM 712 O GLY A 392 18.420 21.184 5.972 1.00 20.90 ATOM 713 N SER A 393 19.087 19.105 6.471 1.00 23.99 ATOM 714 CA SER A 393 18.706 19.178 7.889 1.00 23.62 ATOM 715 CB SER A 393 19.056 17.874 8.593 1.00 20.71 ATOM 716 OG SER A 393 17.926 17.045 8.510 1.00 31.96 ATOM 717 C SER A 393 19.343 20.322 8.656 1.00 17.30 ATOM 718 O SER A 393 18.645 21.149 9.223 1.00 19.88 ATOM 719 N LEU A 394 20.670 20.332 8.677 1.00 20.09 ATOM 720 CA LEU A 394 21.442 21.348 9.365 1.00 21.08 ATOM 721 CB LEU A 394 22.940 21.032 9.274 1.00 19.93 ATOM 722 CG LEU A 394 23.831 20.918 10.516 1.00 26.08 ATOM 723 CD1 LEU A 394 25.207 21.380 10.158 1.00 21.54 ATOM 724 CD2 LEU A 394 23.285 21.730 11.705 1.00 22.96 ATOM 725 C LEU A 394 21.161 22.713 8.753 1.00 23.43 ATOM 726 O LEU A 394 21.132 23.717 9.462 1.00 21.36 ATOM 727 N GLU A 395 20.942 22.759 7.436 1.00 22.13 ATOM 728 CA GLU A 395 20.642 24.037 6.787 1.00 20.91 ATOM 729 CB GLU A 395 20.574 23.890 5.260 1.00 22.76 ATOM 730 CG GLU A 395 21.881 23.459 4.611 1.00 23.62 ATOM 731 CD GLU A 395 21.809 23.461 3.084 1.00 26.69 ATOM 732 OE1 GLU A 395 22.852 23.482 2.434 1.00 27.60 ATOM 733 OE2 GLU A 395 20.709 23.428 2.526 1.00 22.32 ATOM 734 C GLU A 395 19.342 24.632 7.318 1.00 18.31 ATOM 735 O GLU A 395 19.270 25.832 7.574 1.00 20.03 ATOM 736 N VAL A 396 18.311 23.810 7.498 1.00 18.03 ATOM 737 CA VAL A 396 17.043 24.331 8.031 1.00 24.17 ATOM 738 CB VAL A 396 15.891 23.342 7.818 1.00 20.05 ATOM 739 CG1 VAL A 396 14.587 23.854 8.517 1.00 18.41 ATOM 740 CG2 VAL A 396 15.663 23.177 6.288 1.00 22.83 ATOM 741 C VAL A 396 17.174 24.744 9.525 1.00 25.12 ATOM 742 O VAL A 396 16.476 25.639 10.006 1.00 26.40 ATOM 743 N VAL A 397 18.077 24.073 10.232 1.00 23.34 ATOM 744 CA VAL A 397 18.358 24.401 11.617 1.00 18.37 ATOM 745 CB VAL A 397 19.296 23.338 12.232 1.00 19.79 ATOM 746 CG1 VAL A 397 19.915 23.829 13.534 1.00 20.93 ATOM 747 CG2 VAL A 397 18.517 22.069 12.472 1.00 16.14 ATOM 748 C VAL A 397 19.006 25.802 11.635 1.00 17.79 ATOM 749 O VAL A 397 18.547 26.676 12.359 1.00 21.81 ATOM 750 N PHE A 398 19.981 26.058 10.760 1.00 16.57 ATOM 751 CA PHE A 398 20.625 27.355 10.735 1.00 12.50 ATOM 752 CB PHE A 398 21.910 27.288 9.955 1.00 16.85 ATOM 753 CG PHE A 398 23.017 26.588 10.669 1.00 22.50 ATOM 754 CD1 PHE A 398 23.316 26.899 11.986 1.00 21.63 ATOM 755 CD2 PHE A 398 23.796 25.645 10.014 1.00 21.83 ATOM 756 CE1 PHE A 398 24.375 26.279 12.623 1.00 22.54 ATOM 757 CE2 PHE A 398 24.859 25.021 10.652 1.00 23.29 ATOM 758 CZ PHE A 398 25.151 25.334 11.953 1.00 22.58 ATOM 759 C PHE A 398 19.718 28.486 10.249 1.00 19.24 ATOM 760 O PHE A 398 19.944 29.669 10.570 1.00 19.14 ATOM 761 N ILE A 399 18.663 28.138 9.513 1.00 20.43 ATOM 762 CA ILE A 399 17.685 29.145 9.077 1.00 21.75 ATOM 763 CB ILE A 399 16.790 28.652 7.848 1.00 23.69 ATOM 764 CG2 ILE A 399 15.574 29.562 7.656 1.00 17.51 ATOM 765 CG1 ILE A 399 17.608 28.583 6.538 1.00 26.64 ATOM 766 CD1 ILE A 399 16.942 27.745 5.397 1.00 17.97 ATOM 767 C ILE A 399 16.771 29.382 10.296 1.00 18.17 ATOM 768 O ILE A 399 16.484 30.507 10.662 1.00 20.59 ATOM 769 N ARG A 400 16.317 28.307 10.921 1.00 19.22 ATOM 770 CA ARG A 400 15.451 28.415 12.087 1.00 20.62 ATOM 771 CB ARG A 400 15.000 27.029 12.553 1.00 17.24 ATOM 772 CG ARG A 400 13.783 26.537 11.852 1.00 15.74 ATOM 773 CD ARG A 400 13.420 25.143 12.246 1.00 17.01 ATOM 774 NE ARG A 400 12.189 24.760 11.553 1.00 21.84 ATOM 775 CZ ARG A 400 11.371 23.775 11.909 1.00 21.38 ATOM 776 NH1 ARG A 400 11.643 23.021 12.976 1.00 27.51 ATOM 777 NH2 ARG A 400 10.221 23.610 11.261 1.00 19.58 ATOM 778 C ARG A 400 16.132 29.177 13.235 1.00 22.12 ATOM 779 O ARG A 400 15.456 29.834 14.016 1.00 22.87 ATOM 780 N MET A 401 17.462 29.140 13.283 1.00 20.39 ATOM 781 CA MET A 401 18.251 29.813 14.320 1.00 22.78 ATOM 782 CB MET A 401 19.740 29.612 14.026 1.00 21.38 ATOM 783 CG MET A 401 20.681 30.082 15.096 1.00 17.22 ATOM 784 SD MET A 401 22.356 30.190 14.524 1.00 24.87 ATOM 785 CE MET A 401 22.858 28.674 14.579 1.00 30.52 ATOM 786 C MET A 401 17.942 31.308 14.448 1.00 27.16 ATOM 787 O MET A 401 18.177 31.913 15.495 1.00 24.54 ATOM 788 N CYS A 402 17.451 31.901 13.362 1.00 28.58 ATOM 789 CA CYS A 402 17.102 33.327 13.340 1.00 33.94 ATOM 790 CB CYS A 402 16.827 33.801 11.911 1.00 34.97 ATOM 791 SG CYS A 402 18.382 33.864 11.142 1.00 54.57 ATOM 792 C CYS A 402 15.947 33.699 14.236 1.00 33.06 ATOM 793 O CYS A 402 15.871 34.838 14.722 1.00 36.03 ATOM 794 N ARG A 403 15.033 32.759 14.438 1.00 30.48 ATOM 795 CA ARG A 403 13.903 33.013 15.316 1.00 30.17 ATOM 796 CB ARG A 403 12.846 31.936 15.165 1.00 27.27 ATOM 797 CG ARG A 403 12.529 31.529 13.760 1.00 32.18 ATOM 798 CD ARG A 403 11.217 30.784 13.777 1.00 32.00 ATOM 799 NE ARG A 403 11.202 29.740 14.794 1.00 37.42 ATOM 800 CZ ARG A 403 10.188 29.482 15.616 1.00 33.92 ATOM 801 NH1 ARG A 403 9.078 30.195 15.575 1.00 34.55 ATOM 802 NH2 ARG A 403 10.257 28.436 16.428 1.00 42.16 ATOM 803 C ARG A 403 14.368 32.993 16.780 1.00 29.68 ATOM 804 O ARG A 403 13.653 33.472 17.649 1.00 30.31 ATOM 805 N ALA A 404 15.556 32.431 17.016 1.00 26.70 ATOM 806 CA ALA A 404 16.145 32.267 18.336 1.00 21.83 ATOM 807 CB ALA A 404 16.328 30.768 18.612 1.00 17.43 ATOM 808 C ALA A 404 17.490 32.962 18.394 1.00 23.99 ATOM 809 O ALA A 404 18.371 32.543 19.134 1.00 26.66 ATOM 810 N PHE A 405 17.694 33.990 17.573 1.00 26.59 ATOM 811 CA PHE A 405 18.977 34.705 17.557 1.00 24.98 ATOM 812 CB PHE A 405 19.713 34.470 16.227 1.00 18.47 ATOM 813 CG PHE A 405 21.110 35.018 16.187 1.00 17.64 ATOM 814 CD1 PHE A 405 22.202 34.177 16.313 1.00 16.69 ATOM 815 CD2 PHE A 405 21.345 36.370 15.956 1.00 19.09 ATOM 816 CE1 PHE A 405 23.514 34.669 16.199 1.00 21.32 ATOM 817 CE2 PHE A 405 22.651 36.871 15.841 1.00 17.33 ATOM 818 CZ PHE A 405 23.734 36.032 15.957 1.00 19.99 ATOM 819 C PHE A 405 18.765 36.197 17.805 1.00 28.98 ATOM 820 O PHE A 405 17.845 36.789 17.256 1.00 31.78 ATOM 821 N ASP A 406 19.581 36.763 18.703 1.00 31.70 ATOM 822 CA ASP A 406 19.556 38.180 19.084 1.00 30.27 ATOM 823 CB ASP A 406 19.786 38.339 20.598 1.00 30.55 ATOM 824 CG ASP A 406 19.689 39.798 21.081 1.00 34.22 ATOM 825 OD1 ASP A 406 19.722 40.747 20.278 1.00 31.76 ATOM 826 OD2 ASP A 406 19.575 40.004 22.299 1.00 33.44 ATOM 827 C ASP A 406 20.671 38.897 18.330 1.00 29.96 ATOM 828 O ASP A 406 21.821 38.953 18.804 1.00 29.82 ATOM 829 N SER A 407 20.302 39.510 17.203 1.00 28.41 ATOM 830 CA SER A 407 21.263 40.224 16.374 1.00 34.69 ATOM 831 CB SER A 407 20.597 40.719 15.093 1.00 37.05 ATOM 832 OG SER A 407 21.531 40.766 14.018 1.00 51.86 ATOM 833 C SER A 407 21.922 41.381 17.115 1.00 34.14 ATOM 834 O SER A 407 23.147 41.501 17.139 1.00 35.01 ATOM 835 N GLN A 408 21.113 42.206 17.764 1.00 38.76 ATOM 836 CA GLN A 408 21.632 43.345 18.519 1.00 40.20 ATOM 837 CB GLN A 408 20.516 43.981 19.353 1.00 48.77 ATOM 838 CG GLN A 408 19.250 44.338 18.577 1.00 63.31 ATOM 839 CD GLN A 408 18.001 44.400 19.467 1.00 70.33 ATOM 840 OE1 GLN A 408 17.761 45.387 20.175 1.00 73.70 ATOM 841 NE2 GLN A 408 17.185 43.347 19.405 1.00 72.43 ATOM 842 C GLN A 408 22.744 42.908 19.463 1.00 36.52 ATOM 843 O GLN A 408 23.827 43.493 19.484 1.00 36.77 ATOM 844 N ASN A 409 22.514 41.803 20.156 1.00 32.86 ATOM 845 CA ASN A 409 23.466 41.338 21.132 1.00 31.16 ATOM 846 CB ASN A 409 22.722 41.083 22.438 1.00 34.90 ATOM 847 CG ASN A 409 22.115 42.371 23.024 1.00 35.74 ATOM 848 OD1 ASN A 409 22.850 43.282 23.401 1.00 38.31 ATOM 849 ND2 ASN A 409 20.784 42.457 23.076 1.00 31.20 ATOM 850 C ASN A 409 24.369 40.175 20.752 1.00 32.11 ATOM 851 O ASN A 409 25.179 39.729 21.574 1.00 34.18 ATOM 852 N ASN A 410 24.291 39.743 19.494 1.00 29.63 ATOM 853 CA ASN A 410 25.128 38.646 18.979 1.00 27.78 ATOM 854 CB ASN A 410 26.597 39.063 18.877 1.00 24.50 ATOM 855 CG ASN A 410 27.360 38.235 17.866 1.00 25.12 ATOM 856 OD1 ASN A 410 26.851 37.955 16.780 1.00 29.04 ATOM 857 ND2 ASN A 410 28.568 37.813 18.224 1.00 27.47 ATOM 858 C ASN A 410 25.016 37.476 19.928 1.00 28.72 ATOM 859 O ASN A 410 26.016 36.970 20.457 1.00 27.57 ATOM 860 N THR A 411 23.813 36.948 20.020 1.00 27.68 ATOM 861 CA THR A 411 23.602 35.905 20.977 1.00 26.24 ATOM 862 CB THR A 411 23.208 36.681 22.253 1.00 27.76 ATOM 863 OG1 THR A 411 24.162 36.446 23.305 1.00 31.38 ATOM 864 CG2 THR A 411 21.784 36.514 22.604 1.00 16.40 ATOM 865 C THR A 411 22.577 34.896 20.464 1.00 22.40 ATOM 866 O THR A 411 21.649 35.282 19.779 1.00 24.61 ATOM 867 N VAL A 412 22.768 33.612 20.771 1.00 20.76 ATOM 868 CA VAL A 412 21.857 32.528 20.343 1.00 19.57 ATOM 869 CB VAL A 412 22.607 31.487 19.475 1.00 19.83 ATOM 870 CG1 VAL A 412 21.655 30.780 18.524 1.00 18.01 ATOM 871 CG2 VAL A 412 23.691 32.130 18.740 1.00 33.67 ATOM 872 C VAL A 412 21.278 31.708 21.508 1.00 18.12 ATOM 873 O VAL A 412 22.009 31.325 22.411 1.00 23.18 ATOM 874 N TYR A 413 19.990 31.386 21.453 1.00 16.25 ATOM 875 CA TYR A 413 19.320 30.575 22.465 1.00 17.45 ATOM 876 CB TYR A 413 17.855 30.512 22.122 1.00 17.78 ATOM 877 CG TYR A 413 16.935 29.951 23.181 1.00 25.60 ATOM 878 CD1 TYR A 413 17.039 30.319 24.529 1.00 24.61 ATOM 879 CE1 TYR A 413 16.122 29.840 25.472 1.00 21.19 ATOM 880 CD2 TYR A 413 15.906 29.103 22.819 1.00 24.64 ATOM 881 CE2 TYR A 413 14.991 28.629 23.739 1.00 26.94 ATOM 882 CZ TYR A 413 15.097 28.993 25.065 1.00 28.21 ATOM 883 OH TYR A 413 14.145 28.487 25.945 1.00 27.94 ATOM 884 C TYR A 413 19.906 29.164 22.453 1.00 23.48 ATOM 885 O TYR A 413 19.656 28.401 21.518 1.00 24.97 ATOM 886 N PHE A 414 20.684 28.828 23.488 1.00 22.58 ATOM 887 CA PHE A 414 21.360 27.534 23.625 1.00 21.94 ATOM 888 CB PHE A 414 22.835 27.685 23.195 1.00 18.84 ATOM 889 CG PHE A 414 23.734 26.507 23.555 1.00 23.28 ATOM 890 CD1 PHE A 414 23.637 25.283 22.871 1.00 23.77 ATOM 891 CD2 PHE A 414 24.718 26.634 24.556 1.00 20.51 ATOM 892 CE1 PHE A 414 24.510 24.201 23.178 1.00 25.81 ATOM 893 CE2 PHE A 414 25.586 25.569 24.865 1.00 17.09 ATOM 894 CZ PHE A 414 25.483 24.350 24.178 1.00 23.54 ATOM 895 C PHE A 414 21.303 26.977 25.057 1.00 25.66 ATOM 896 O PHE A 414 21.612 27.677 26.024 1.00 22.04 ATOM 897 N ASP A 415 20.866 25.731 25.196 1.00 25.08 ATOM 898 CA ASP A 415 20.849 25.114 26.513 1.00 22.21 ATOM 899 CB ASP A 415 22.303 24.853 26.921 1.00 17.07 ATOM 900 CG ASP A 415 22.441 23.735 27.894 1.00 18.13 ATOM 901 OD1 ASP A 415 21.457 23.014 28.110 1.00 18.33 ATOM 902 OD2 ASP A 415 23.551 23.579 28.420 1.00 20.42 ATOM 903 C ASP A 415 20.130 25.970 27.579 1.00 25.14 ATOM 904 O ASP A 415 20.700 26.259 28.633 1.00 29.15 ATOM 905 N GLY A 416 18.912 26.408 27.269 1.00 20.65 ATOM 906 CA GLY A 416 18.118 27.176 28.201 1.00 18.89 ATOM 907 C GLY A 416 18.258 28.682 28.257 1.00 13.58 ATOM 908 O GLY A 416 17.349 29.327 28.744 1.00 19.33 ATOM 909 N LYS A 417 19.364 29.254 27.817 1.00 14.55 ATOM 910 CA LYS A 417 19.498 30.716 27.861 1.00 18.31 ATOM 911 CB LYS A 417 20.345 31.134 29.074 1.00 20.71 ATOM 912 CG LYS A 417 19.682 30.877 30.428 1.00 22.06 ATOM 913 CD LYS A 417 20.679 31.167 31.538 1.00 23.89 ATOM 914 CE LYS A 417 19.970 31.232 32.891 1.00 26.28 ATOM 915 NZ LYS A 417 20.937 31.696 33.916 1.00 27.48 ATOM 916 C LYS A 417 20.183 31.202 26.592 1.00 23.82 ATOM 917 O LYS A 417 20.635 30.382 25.781 1.00 21.77 ATOM 918 N TYR A 418 20.315 32.526 26.443 1.00 21.57 ATOM 919 CA TYR A 418 20.972 33.115 25.270 1.00 19.31 ATOM 920 CB TYR A 418 20.369 34.492 24.921 1.00 18.21 ATOM 921 CG TYR A 418 19.066 34.407 24.142 1.00 21.12 ATOM 922 CD1 TYR A 418 17.856 34.087 24.777 1.00 18.03 ATOM 923 CE1 TYR A 418 16.682 33.930 24.048 1.00 22.16 ATOM 924 CD2 TYR A 418 19.060 34.576 22.743 1.00 19.41 ATOM 925 CE2 TYR A 418 17.903 34.419 22.007 1.00 16.83 ATOM 926 CZ TYR A 418 16.728 34.099 22.648 1.00 24.12 ATOM 927 OH TYR A 418 15.601 33.944 21.890 1.00 22.47 ATOM 928 C TYR A 418 22.471 33.183 25.451 1.00 19.85 ATOM 929 O TYR A 418 22.974 33.820 26.385 1.00 25.51 ATOM 930 N ALA A 419 23.180 32.482 24.570 1.00 16.24 ATOM 931 CA ALA A 419 24.630 32.365 24.577 1.00 15.65 ATOM 932 CB ALA A 419 24.986 30.903 24.326 1.00 17.04 ATOM 933 C ALA A 419 25.463 33.245 23.629 1.00 25.93 ATOM 934 O ALA A 419 25.168 33.359 22.432 1.00 27.89 ATOM 935 N SER A 420 26.540 33.817 24.157 1.00 23.17 ATOM 936 CA SER A 420 27.455 34.619 23.360 1.00 24.99 ATOM 937 CB SER A 420 28.202 35.577 24.280 1.00 27.55 ATOM 938 OG SER A 420 29.050 34.861 25.170 1.00 31.44 ATOM 939 C SER A 420 28.442 33.622 22.735 1.00 25.61 ATOM 940 O SER A 420 28.462 32.461 23.132 1.00 26.24 ATOM 941 N PRO A 421 29.267 34.040 21.748 1.00 27.91 ATOM 942 CD PRO A 421 29.281 35.313 20.998 1.00 28.16 ATOM 943 CA PRO A 421 30.209 33.071 21.160 1.00 27.21 ATOM 944 CB PRO A 421 31.014 33.928 20.178 1.00 25.80 ATOM 945 CG PRO A 421 30.031 34.959 19.743 1.00 24.69 ATOM 946 C PRO A 421 31.158 32.380 22.163 1.00 34.03 ATOM 947 O PRO A 421 31.509 31.199 21.988 1.00 31.00 ATOM 948 N ASP A 422 31.627 33.142 23.158 1.00 33.32 ATOM 949 CA ASP A 422 32.570 32.623 24.154 1.00 35.81 ATOM 950 CB ASP A 422 33.136 33.742 25.030 1.00 44.04 ATOM 951 CG ASP A 422 32.246 34.946 25.069 1.00 54.68 ATOM 952 OD1 ASP A 422 32.454 35.892 24.251 1.00 54.42 ATOM 953 OD2 ASP A 422 31.327 34.920 25.913 1.00 58.40 ATOM 954 C ASP A 422 32.104 31.415 24.972 1.00 29.08 ATOM 955 O ASP A 422 32.923 30.698 25.550 1.00 29.48 ATOM 956 N VAL A 423 30.796 31.180 24.968 1.00 24.96 ATOM 957 CA VAL A 423 30.197 30.031 25.620 1.00 22.62 ATOM 958 CB VAL A 423 28.671 30.120 25.495 1.00 19.09 ATOM 959 CG1 VAL A 423 28.025 28.771 25.617 1.00 20.56 ATOM 960 CG2 VAL A 423 28.115 31.068 26.536 1.00 21.12 ATOM 961 C VAL A 423 30.724 28.783 24.894 1.00 26.71 ATOM 962 O VAL A 423 30.975 27.746 25.499 1.00 24.85 ATOM 963 N PHE A 424 31.040 28.951 23.611 1.00 26.18 ATOM 964 CA PHE A 424 31.507 27.854 22.774 1.00 22.48 ATOM 965 CB PHE A 424 30.860 27.963 21.371 1.00 23.86 ATOM 966 CG PHE A 424 29.341 28.011 21.394 1.00 20.24 ATOM 967 CD1 PHE A 424 28.668 29.227 21.384 1.00 15.91 ATOM 968 CD2 PHE A 424 28.598 26.843 21.509 1.00 15.76 ATOM 969 CE1 PHE A 424 27.290 29.270 21.500 1.00 16.18 ATOM 970 CE2 PHE A 424 27.238 26.880 21.623 1.00 13.58 ATOM 971 CZ PHE A 424 26.573 28.099 21.624 1.00 16.90 ATOM 972 C PHE A 424 33.014 27.757 22.663 1.00 23.66 ATOM 973 O PHE A 424 33.539 26.929 21.911 1.00 24.93 ATOM 974 N LYS A 425 33.727 28.552 23.451 1.00 26.33 ATOM 975 CA LYS A 425 35.186 28.527 23.392 1.00 29.12 ATOM 976 CB LYS A 425 35.776 29.467 24.452 1.00 32.35 ATOM 977 CG LYS A 425 37.306 29.529 24.457 1.00 31.98 ATOM 978 CD LYS A 425 37.762 30.593 25.418 1.00 39.70 ATOM 979 CE LYS A 425 39.265 30.718 25.450 1.00 48.00 ATOM 980 NZ LYS A 425 39.725 31.844 26.336 1.00 53.67 ATOM 981 C LYS A 425 35.889 27.157 23.476 1.00 31.57 ATOM 982 O LYS A 425 36.792 26.863 22.673 1.00 27.27 ATOM 983 N SER A 426 35.521 26.339 24.465 1.00 30.78 ATOM 984 CA SER A 426 36.182 25.050 24.607 1.00 33.82 ATOM 985 CB SER A 426 35.862 24.390 25.959 1.00 30.28 ATOM 986 OG SER A 426 34.486 24.161 26.133 1.00 37.92 ATOM 987 C SER A 426 35.992 24.104 23.417 1.00 35.48 ATOM 988 O SER A 426 36.713 23.122 23.286 1.00 37.65 ATOM 989 N LEU A 427 35.109 24.463 22.488 1.00 35.14 ATOM 990 CA LEU A 427 34.879 23.644 21.300 1.00 33.29 ATOM 991 CB LEU A 427 33.771 24.270 20.461 1.00 30.08 ATOM 992 CG LEU A 427 32.682 23.462 19.781 1.00 28.00 ATOM 993 CD1 LEU A 427 32.151 22.380 20.671 1.00 25.88 ATOM 994 CD2 LEU A 427 31.574 24.418 19.397 1.00 25.10 ATOM 995 C LEU A 427 36.166 23.655 20.494 1.00 33.91 ATOM 996 O LEU A 427 36.533 22.656 19.901 1.00 36.72 ATOM 997 N GLY A 428 36.862 24.790 20.503 1.00 39.65 ATOM 998 CA GLY A 428 38.105 24.932 19.750 1.00 40.93 ATOM 999 C GLY A 428 37.884 25.241 18.269 1.00 43.39 ATOM 1000 O GLY A 428 38.806 25.108 17.455 1.00 42.81 ATOM 1001 N CYS A 429 36.670 25.685 17.927 1.00 43.35 ATOM 1002 CA CYS A 429 36.291 25.995 16.544 1.00 43.84 ATOM 1003 CB CYS A 429 35.025 25.224 16.176 1.00 43.95 ATOM 1004 SG CYS A 429 35.244 23.452 16.181 1.00 50.28 ATOM 1005 C CYS A 429 36.012 27.475 16.409 1.00 42.57 ATOM 1006 O CYS A 429 35.003 27.873 15.838 1.00 39.45 ATOM 1007 N GLU A 430 36.934 28.292 16.901 1.00 43.43 ATOM 1008 CA GLU A 430 36.761 29.740 16.874 1.00 45.32 ATOM 1009 CB GLU A 430 38.051 30.447 17.301 1.00 53.81 ATOM 1010 CG GLU A 430 38.849 29.738 18.439 1.00 70.87 ATOM 1011 CD GLU A 430 38.051 29.456 19.737 1.00 77.73 ATOM 1012 OE1 GLU A 430 37.138 30.245 20.098 1.00 80.51 ATOM 1013 OE2 GLU A 430 38.365 28.437 20.408 1.00 78.46 ATOM 1014 C GLU A 430 36.236 30.320 15.552 1.00 40.15 ATOM 1015 O GLU A 430 35.304 31.127 15.563 1.00 35.32 ATOM 1016 N ASP A 431 36.782 29.870 14.420 1.00 36.97 ATOM 1017 CA ASP A 431 36.355 30.383 13.101 1.00 37.50 ATOM 1018 CB ASP A 431 37.352 30.007 12.009 1.00 45.12 ATOM 1019 CG ASP A 431 38.743 30.507 12.303 1.00 50.38 ATOM 1020 OD1 ASP A 431 39.005 31.715 12.088 1.00 52.92 ATOM 1021 OD2 ASP A 431 39.564 29.686 12.767 1.00 58.71 ATOM 1022 C ASP A 431 34.953 29.983 12.668 1.00 31.17 ATOM 1023 O ASP A 431 34.169 30.832 12.249 1.00 29.39 ATOM 1024 N PHE A 432 34.642 28.697 12.805 1.00 25.82 ATOM 1025 CA PHE A 432 33.334 28.162 12.467 1.00 24.06 ATOM 1026 CB PHE A 432 33.343 26.640 12.666 1.00 23.24 ATOM 1027 CG PHE A 432 31.981 26.008 12.634 1.00 26.00 ATOM 1028 CD1 PHE A 432 31.359 25.728 11.428 1.00 24.09 ATOM 1029 CD2 PHE A 432 31.301 25.727 13.826 1.00 24.00 ATOM 1030 CE1 PHE A 432 30.077 25.182 11.407 1.00 25.60 ATOM 1031 CE2 PHE A 432 30.017 25.182 13.819 1.00 23.27 ATOM 1032 CZ PHE A 432 29.399 24.907 12.608 1.00 27.15 ATOM 1033 C PHE A 432 32.290 28.823 13.368 1.00 24.49 ATOM 1034 O PHE A 432 31.166 29.081 12.939 1.00 23.40 ATOM 1035 N ILE A 433 32.667 29.123 14.614 1.00 23.33 ATOM 1036 CA ILE A 433 31.729 29.746 15.545 1.00 21.41 ATOM 1037 CB ILE A 433 32.226 29.697 17.038 1.00 24.82 ATOM 1038 CG2 ILE A 433 31.307 30.551 17.946 1.00 24.79 ATOM 1039 CG1 ILE A 433 32.233 28.244 17.554 1.00 22.78 ATOM 1040 CD1 ILE A 433 30.846 27.630 17.696 1.00 21.04 ATOM 1041 C ILE A 433 31.453 31.179 15.113 1.00 17.19 ATOM 1042 O ILE A 433 30.293 31.589 15.046 1.00 21.19 ATOM 1043 N SER A 434 32.491 31.937 14.770 1.00 23.08 ATOM 1044 CA SER A 434 32.257 33.319 14.327 1.00 25.60 ATOM 1045 CB SER A 434 33.561 34.097 14.162 1.00 28.06 ATOM 1046 OG SER A 434 34.547 33.294 13.558 1.00 37.81 ATOM 1047 C SER A 434 31.465 33.276 13.028 1.00 23.82 ATOM 1048 O SER A 434 30.564 34.072 12.821 1.00 23.76 ATOM 1049 N PHE A 435 31.752 32.279 12.199 1.00 24.82 ATOM 1050 CA PHE A 435 31.034 32.096 10.947 1.00 24.08 ATOM 1051 CB PHE A 435 31.646 30.923 10.161 1.00 26.80 ATOM 1052 CG PHE A 435 31.106 30.767 8.748 1.00 30.19 ATOM 1053 CD1 PHE A 435 30.205 31.686 8.209 1.00 35.50 ATOM 1054 CD2 PHE A 435 31.487 29.678 7.961 1.00 33.97 ATOM 1055 CE1 PHE A 435 29.684 31.523 6.906 1.00 34.39 ATOM 1056 CE2 PHE A 435 30.977 29.505 6.657 1.00 34.83 ATOM 1057 CZ PHE A 435 30.074 30.430 6.136 1.00 31.71 ATOM 1058 C PHE A 435 29.548 31.844 11.264 1.00 26.45 ATOM 1059 O PHE A 435 28.665 32.480 10.688 1.00 28.86 ATOM 1060 N VAL A 436 29.255 30.967 12.223 1.00 22.48 ATOM 1061 CA VAL A 436 27.865 30.691 12.559 1.00 17.41 ATOM 1062 CB VAL A 436 27.757 29.624 13.695 1.00 17.64 ATOM 1063 CG1 VAL A 436 26.377 29.570 14.228 1.00 22.49 ATOM 1064 CG2 VAL A 436 28.122 28.278 13.195 1.00 17.15 ATOM 1065 C VAL A 436 27.164 31.978 12.991 1.00 17.44 ATOM 1066 O VAL A 436 26.053 32.278 12.534 1.00 18.61 ATOM 1067 N PHE A 437 27.803 32.741 13.874 1.00 19.96 ATOM 1068 CA PHE A 437 27.184 33.971 14.362 1.00 22.62 ATOM 1069 CB PHE A 437 27.946 34.539 15.573 1.00 24.58 ATOM 1070 CG PHE A 437 27.559 33.905 16.891 1.00 23.31 ATOM 1071 CD1 PHE A 437 27.912 32.593 17.180 1.00 24.58 ATOM 1072 CD2 PHE A 437 26.855 34.627 17.841 1.00 23.23 ATOM 1073 CE1 PHE A 437 27.572 32.012 18.402 1.00 22.25 ATOM 1074 CE2 PHE A 437 26.514 34.055 19.059 1.00 23.56 ATOM 1075 CZ PHE A 437 26.874 32.746 19.334 1.00 18.83 ATOM 1076 C PHE A 437 27.010 35.034 13.274 1.00 22.54 ATOM 1077 O PHE A 437 25.985 35.716 13.232 1.00 27.26 ATOM 1078 N GLU A 438 28.001 35.176 12.400 1.00 26.36 ATOM 1079 CA GLU A 438 27.898 36.157 11.302 1.00 27.43 ATOM 1080 CB GLU A 438 29.164 36.179 10.440 1.00 30.05 ATOM 1081 CG GLU A 438 29.073 37.131 9.227 1.00 31.17 ATOM 1082 CD GLU A 438 30.417 37.447 8.605 1.00 31.35 ATOM 1083 OE1 GLU A 438 31.384 36.685 8.801 1.00 27.62 ATOM 1084 OE2 GLU A 438 30.509 38.491 7.932 1.00 40.19 ATOM 1085 C GLU A 438 26.674 35.839 10.450 1.00 25.73 ATOM 1086 O GLU A 438 25.918 36.730 10.093 1.00 28.14 ATOM 1087 N PHE A 439 26.449 34.555 10.188 1.00 26.08 ATOM 1088 CA PHE A 439 25.292 34.118 9.433 1.00 24.60 ATOM 1089 CB PHE A 439 25.398 32.619 9.135 1.00 26.02 ATOM 1090 CG PHE A 439 24.280 32.098 8.283 1.00 27.70 ATOM 1091 CD1 PHE A 439 24.304 32.270 6.904 1.00 29.06 ATOM 1092 CD2 PHE A 439 23.177 31.483 8.855 1.00 31.10 ATOM 1093 CE1 PHE A 439 23.251 31.842 6.123 1.00 24.89 ATOM 1094 CE2 PHE A 439 22.111 31.050 8.069 1.00 31.13 ATOM 1095 CZ PHE A 439 22.153 31.234 6.701 1.00 28.01 ATOM 1096 C PHE A 439 23.964 34.426 10.162 1.00 28.45 ATOM 1097 O PHE A 439 22.958 34.770 9.518 1.00 28.20 ATOM 1098 N GLY A 440 23.926 34.257 11.491 1.00 26.29 ATOM 1099 CA GLY A 440 22.699 34.550 12.217 1.00 20.95 ATOM 1100 C GLY A 440 22.380 36.035 12.079 1.00 24.76 ATOM 1101 O GLY A 440 21.247 36.459 11.831 1.00 24.56 ATOM 1102 N LYS A 441 23.409 36.842 12.249 1.00 25.11 ATOM 1103 CA LYS A 441 23.283 38.290 12.135 1.00 31.81 ATOM 1104 CB LYS A 441 24.674 38.871 12.293 1.00 34.53 ATOM 1105 CG LYS A 441 24.720 40.343 12.482 1.00 48.07 ATOM 1106 CD LYS A 441 25.618 40.643 13.668 1.00 58.50 ATOM 1107 CE LYS A 441 25.088 39.955 14.934 1.00 61.35 ATOM 1108 NZ LYS A 441 25.698 40.550 16.152 1.00 67.81 ATOM 1109 C LYS A 441 22.741 38.659 10.733 1.00 34.70 ATOM 1110 O LYS A 441 21.767 39.411 10.579 1.00 32.85 ATOM 1111 N SER A 442 23.408 38.091 9.729 1.00 33.69 ATOM 1112 CA SER A 442 23.113 38.278 8.312 1.00 32.10 ATOM 1113 CB SER A 442 24.060 37.413 7.493 1.00 34.00 ATOM 1114 OG SER A 442 23.706 37.415 6.142 1.00 42.63 ATOM 1115 C SER A 442 21.699 37.939 7.953 1.00 29.45 ATOM 1116 O SER A 442 21.022 38.710 7.283 1.00 28.07 ATOM 1117 N LEU A 443 21.252 36.769 8.383 1.00 30.75 ATOM 1118 CA LEU A 443 19.903 36.341 8.091 1.00 28.97 ATOM 1119 CB LEU A 443 19.754 34.844 8.362 1.00 32.66 ATOM 1120 CG LEU A 443 19.232 33.966 7.225 1.00 34.63 ATOM 1121 CD1 LEU A 443 19.001 32.579 7.758 1.00 34.61 ATOM 1122 CD2 LEU A 443 17.933 34.502 6.669 1.00 35.80 ATOM 1123 C LEU A 443 18.900 37.163 8.897 1.00 33.40 ATOM 1124 O LEU A 443 17.761 37.366 8.461 1.00 31.79 ATOM 1125 N CYS A 444 19.330 37.656 10.063 1.00 39.70 ATOM 1126 CA CYS A 444 18.474 38.478 10.937 1.00 44.50 ATOM 1127 CB CYS A 444 19.117 38.687 12.312 1.00 50.28 ATOM 1128 SG CYS A 444 18.752 37.411 13.539 1.00 54.66 ATOM 1129 C CYS A 444 18.177 39.845 10.346 1.00 44.03 ATOM 1130 O CYS A 444 17.053 40.343 10.468 1.00 42.14 ATOM 1131 N SER A 445 19.190 40.456 9.733 1.00 43.30 ATOM 1132 CA SER A 445 19.020 41.765 9.118 1.00 47.44 ATOM 1133 CB SER A 445 20.343 42.266 8.518 1.00 48.13 ATOM 1134 OG SER A 445 20.752 41.518 7.383 1.00 50.15 ATOM 1135 C SER A 445 17.885 41.815 8.071 1.00 48.45 ATOM 1136 O SER A 445 17.459 42.901 7.663 1.00 53.44 ATOM 1137 N MET A 446 17.393 40.656 7.636 1.00 44.69 ATOM 1138 CA MET A 446 16.306 40.631 6.665 1.00 43.05 ATOM 1139 CB MET A 446 16.389 39.386 5.789 1.00 40.50 ATOM 1140 CG MET A 446 17.577 39.419 4.842 1.00 41.60 ATOM 1141 SD MET A 446 17.833 37.906 3.917 1.00 47.28 ATOM 1142 CE MET A 446 19.506 37.667 4.191 1.00 42.50 ATOM 1143 C MET A 446 14.953 40.725 7.355 1.00 46.65 ATOM 1144 O MET A 446 13.971 41.150 6.746 1.00 50.18 ATOM 1145 N HIS A 447 14.921 40.382 8.643 1.00 46.34 ATOM 1146 CA HIS A 447 13.702 40.426 9.420 1.00 48.76 ATOM 1147 CB HIS A 447 13.259 41.882 9.589 1.00 60.69 ATOM 1148 CG HIS A 447 12.149 42.066 10.578 1.00 78.35 ATOM 1149 CD2 HIS A 447 11.722 41.273 11.592 1.00 83.48 ATOM 1150 ND1 HIS A 447 11.308 43.163 10.569 1.00 85.45 ATOM 1151 CE1 HIS A 447 10.405 43.032 11.529 1.00 86.49 ATOM 1152 NE2 HIS A 447 10.633 41.893 12.161 1.00 87.93 ATOM 1153 C HIS A 447 12.618 39.583 8.729 1.00 47.17 ATOM 1154 O HIS A 447 11.618 40.114 8.233 1.00 48.76 ATOM 1155 N LEU A 448 12.853 38.272 8.654 1.00 43.85 ATOM 1156 CA LEU A 448 11.922 37.320 8.021 1.00 37.21 ATOM 1157 CB LEU A 448 12.667 36.021 7.633 1.00 36.92 ATOM 1158 CG LEU A 448 14.004 36.045 6.867 1.00 36.45 ATOM 1159 CD1 LEU A 448 14.486 34.629 6.601 1.00 35.34 ATOM 1160 CD2 LEU A 448 13.867 36.798 5.553 1.00 41.17 ATOM 1161 C LEU A 448 10.703 36.961 8.887 1.00 34.64 ATOM 1162 O LEU A 448 10.847 36.731 10.083 1.00 35.66 ATOM 1163 N THR A 449 9.512 36.911 8.288 1.00 31.11 ATOM 1164 CA THR A 449 8.305 36.549 9.033 1.00 28.99 ATOM 1165 CB THR A 449 7.006 36.973 8.313 1.00 30.22 ATOM 1166 OG1 THR A 449 6.777 36.098 7.201 1.00 29.38 ATOM 1167 CG2 THR A 449 7.081 38.431 7.839 1.00 25.55 ATOM 1168 C THR A 449 8.271 35.030 9.134 1.00 29.64 ATOM 1169 O THR A 449 8.953 34.351 8.371 1.00 31.91 ATOM 1170 N GLU A 450 7.479 34.491 10.051 1.00 26.47 ATOM 1171 CA GLU A 450 7.392 33.047 10.182 1.00 27.53 ATOM 1172 CB GLU A 450 6.328 32.679 11.204 1.00 25.91 ATOM 1173 CG GLU A 450 6.730 33.026 12.617 1.00 27.73 ATOM 1174 CD GLU A 450 7.853 32.146 13.117 1.00 24.37 ATOM 1175 OE1 GLU A 450 7.554 31.004 13.513 1.00 29.52 ATOM 1176 OE2 GLU A 450 9.021 32.586 13.108 1.00 28.01 ATOM 1177 C GLU A 450 7.104 32.350 8.844 1.00 29.72 ATOM 1178 O GLU A 450 7.748 31.372 8.492 1.00 29.06 ATOM 1179 N ASP A 451 6.181 32.899 8.070 1.00 32.63 ATOM 1180 CA ASP A 451 5.830 32.306 6.780 1.00 30.31 ATOM 1181 CB ASP A 451 4.615 33.023 6.182 1.00 34.34 ATOM 1182 CG ASP A 451 3.314 32.660 6.891 1.00 39.42 ATOM 1183 OD1 ASP A 451 3.330 31.766 7.755 1.00 42.60 ATOM 1184 OD2 ASP A 451 2.261 33.254 6.573 1.00 46.92 ATOM 1185 C ASP A 451 7.005 32.321 5.813 1.00 27.29 ATOM 1186 O ASP A 451 7.238 31.364 5.090 1.00 27.40 ATOM 1187 N GLU A 452 7.765 33.404 5.821 1.00 29.17 ATOM 1188 CA GLU A 452 8.928 33.510 4.946 1.00 33.64 ATOM 1189 CB GLU A 452 9.521 34.927 5.022 1.00 34.38 ATOM 1190 CG GLU A 452 8.592 35.990 4.410 1.00 38.12 ATOM 1191 CD GLU A 452 9.061 37.426 4.609 1.00 40.47 ATOM 1192 OE1 GLU A 452 10.047 37.667 5.330 1.00 42.73 ATOM 1193 OE2 GLU A 452 8.424 38.339 4.047 1.00 45.30 ATOM 1194 C GLU A 452 9.976 32.432 5.286 1.00 35.02 ATOM 1195 O GLU A 452 10.558 31.814 4.378 1.00 32.26 ATOM 1196 N ILE A 453 10.200 32.209 6.589 1.00 31.95 ATOM 1197 CA ILE A 453 11.159 31.194 7.061 1.00 28.64 ATOM 1198 CB ILE A 453 11.397 31.290 8.615 1.00 31.75 ATOM 1199 CG2 ILE A 453 12.135 30.045 9.139 1.00 28.09 ATOM 1200 CG1 ILE A 453 12.218 32.538 8.952 1.00 29.57 ATOM 1201 CD1 ILE A 453 12.224 32.863 10.422 1.00 27.64 ATOM 1202 C ILE A 453 10.640 29.793 6.707 1.00 25.34 ATOM 1203 O ILE A 453 11.408 28.904 6.331 1.00 27.62 ATOM 1204 N ALA A 454 9.331 29.604 6.834 1.00 25.41 ATOM 1205 CA ALA A 454 8.698 28.317 6.524 1.00 28.05 ATOM 1206 CB ALA A 454 7.194 28.381 6.798 1.00 23.33 ATOM 1207 C ALA A 454 8.941 27.940 5.064 1.00 30.98 ATOM 1208 O ALA A 454 9.408 26.839 4.763 1.00 27.28 ATOM 1209 N LEU A 455 8.696 28.899 4.173 1.00 34.22 ATOM 1210 CA LEU A 455 8.850 28.677 2.744 1.00 33.15 ATOM 1211 CB LEU A 455 8.023 29.706 1.945 1.00 35.88 ATOM 1212 CG LEU A 455 6.504 29.399 1.973 1.00 35.93 ATOM 1213 CD1 LEU A 455 5.706 30.626 1.672 1.00 39.84 ATOM 1214 CD2 LEU A 455 6.159 28.277 0.989 1.00 32.00 ATOM 1215 C LEU A 455 10.307 28.601 2.328 1.00 30.16 ATOM 1216 O LEU A 455 10.676 27.724 1.540 1.00 32.09 ATOM 1217 N PHE A 456 11.150 29.460 2.894 1.00 26.03 ATOM 1218 CA PHE A 456 12.564 29.400 2.561 1.00 25.28 ATOM 1219 CB PHE A 456 13.313 30.595 3.142 1.00 27.10 ATOM 1220 CG PHE A 456 14.766 30.654 2.734 1.00 32.50 ATOM 1221 CD1 PHE A 456 15.151 30.366 1.421 1.00 31.72 ATOM 1222 CD2 PHE A 456 15.754 30.994 3.660 1.00 32.12 ATOM 1223 CE1 PHE A 456 16.484 30.414 1.040 1.00 31.33 ATOM 1224 CE2 PHE A 456 17.097 31.046 3.285 1.00 34.09 ATOM 1225 CZ PHE A 456 17.465 30.755 1.971 1.00 33.73 ATOM 1226 C PHE A 456 13.165 28.073 3.061 1.00 27.08 ATOM 1227 O PHE A 456 14.077 27.522 2.452 1.00 24.18 ATOM 1228 N SER A 457 12.626 27.547 4.162 1.00 26.66 ATOM 1229 CA SER A 457 13.084 26.278 4.719 1.00 24.70 ATOM 1230 CB SER A 457 12.366 25.986 6.034 1.00 22.68 ATOM 1231 OG SER A 457 12.761 26.899 7.025 1.00 28.15 ATOM 1232 C SER A 457 12.734 25.169 3.748 1.00 23.81 ATOM 1233 O SER A 457 13.561 24.315 3.425 1.00 21.55 ATOM 1234 N ALA A 458 11.470 25.154 3.337 1.00 24.49 ATOM 1235 CA ALA A 458 10.992 24.142 2.397 1.00 27.62 ATOM 1236 CB ALA A 458 9.526 24.345 2.126 1.00 26.08 ATOM 1237 C ALA A 458 11.811 24.190 1.095 1.00 25.57 ATOM 1238 O ALA A 458 12.205 23.161 0.571 1.00 28.96 ATOM 1239 N PHE A 459 12.153 25.399 0.660 1.00 27.37 ATOM 1240 CA PHE A 459 12.945 25.642 −0.553 1.00 28.58 ATOM 1241 CB PHE A 459 13.083 27.162 −0.758 1.00 28.53 ATOM 1242 CG PHE A 459 13.907 27.558 −1.956 1.00 33.04 ATOM 1243 CD1 PHE A 459 13.402 27.404 −3.255 1.00 37.29 ATOM 1244 CD2 PHE A 459 15.168 28.122 −1.789 1.00 32.57 ATOM 1245 CE1 PHE A 459 14.142 27.809 −4.360 1.00 33.63 ATOM 1246 CE2 PHE A 459 15.920 28.533 −2.886 1.00 36.16 ATOM 1247 CZ PHE A 459 15.407 28.378 −4.175 1.00 37.49 ATOM 1248 C PHE A 459 14.331 25.008 −0.495 1.00 28.01 ATOM 1249 O PHE A 459 14.743 24.252 −1.372 1.00 29.21 ATOM 1250 N VAL A 460 15.067 25.334 0.553 1.00 29.05 ATOM 1251 CA VAL A 460 16.407 24.798 0.701 1.00 26.40 ATOM 1252 CB VAL A 460 17.143 25.531 1.839 1.00 28.85 ATOM 1253 CG1 VAL A 460 18.470 24.967 2.044 1.00 34.54 ATOM 1254 CG2 VAL A 460 17.319 26.974 1.484 1.00 30.19 ATOM 1255 C VAL A 460 16.385 23.268 0.889 1.00 24.40 ATOM 1256 O VAL A 460 17.295 22.563 0.447 1.00 25.65 ATOM 1257 N LEU A 461 15.307 22.743 1.469 1.00 24.80 ATOM 1258 CA LEU A 461 15.194 21.297 1.700 1.00 26.95 ATOM 1259 CB LEU A 461 14.034 21.015 2.653 1.00 28.61 ATOM 1260 CG LEU A 461 14.024 19.600 3.228 1.00 30.23 ATOM 1261 CD1 LEU A 461 15.049 19.523 4.335 1.00 30.35 ATOM 1262 CD2 LEU A 461 12.637 19.257 3.751 1.00 37.76 ATOM 1263 C LEU A 461 14.966 20.496 0.416 1.00 27.27 ATOM 1264 O LEU A 461 15.566 19.430 0.198 1.00 26.82 ATOM 1265 N MET A 462 14.023 20.991 −0.380 1.00 27.27 ATOM 1266 CA MET A 462 13.650 20.378 −1.640 1.00 30.35 ATOM 1267 CB MET A 462 12.196 20.707 −1.964 1.00 30.76 ATOM 1268 CG MET A 462 11.213 20.255 −0.874 1.00 41.65 ATOM 1269 SD MET A 462 11.153 18.462 −0.489 1.00 43.91 ATOM 1270 CE MET A 462 10.018 17.928 −1.767 1.00 47.33 ATOM 1271 C MET A 462 14.574 20.870 −2.730 1.00 29.93 ATOM 1272 O MET A 462 14.135 21.418 −3.729 1.00 33.71 ATOM 1273 N SER A 463 15.864 20.657 −2.524 1.00 30.81 ATOM 1274 CA SER A 463 16.881 21.064 −3.470 1.00 35.27 ATOM 1275 CB SER A 463 18.143 21.489 −2.730 1.00 36.89 ATOM 1276 OG SER A 463 18.963 22.273 −3.578 1.00 50.70 ATOM 1277 C SER A 463 17.174 19.889 −4.411 1.00 36.64 ATOM 1278 O SER A 463 17.599 18.819 −3.976 1.00 32.89 ATOM 1279 N ALA A 464 16.925 20.096 −5.702 1.00 39.89 ATOM 1280 CA ALA A 464 17.127 19.053 −6.698 1.00 40.73 ATOM 1281 CB ALA A 464 16.425 19.425 −7.980 1.00 39.42 ATOM 1282 C ALA A 464 18.585 18.728 −6.969 1.00 42.63 ATOM 1283 O ALA A 464 18.897 17.616 −7.401 1.00 48.91 ATOM 1284 N ASP A 465 19.481 19.663 −6.656 1.00 43.62 ATOM 1285 CA ASP A 465 20.905 19.461 −6.908 1.00 43.08 ATOM 1286 CB ASP A 465 21.546 20.754 −7.398 1.00 49.21 ATOM 1287 CG ASP A 465 21.620 21.805 −6.324 1.00 54.48 ATOM 1288 OD1 ASP A 465 22.753 22.243 −6.029 1.00 56.04 ATOM 1289 OD2 ASP A 465 20.555 22.184 −5.783 1.00 57.56 ATOM 1290 C ASP A 465 21.766 18.855 −5.803 1.00 41.94 ATOM 1291 O ASP A 465 22.946 19.191 −5.677 1.00 46.76 ATOM 1292 N ARG A 466 21.190 17.995 −4.976 1.00 37.97 ATOM 1293 CA ARG A 466 21.987 17.342 −3.953 1.00 34.33 ATOM 1294 CB ARG A 466 21.112 16.818 −2.804 1.00 31.22 ATOM 1295 CG ARG A 466 20.380 17.869 −2.006 1.00 27.68 ATOM 1296 CD ARG A 466 21.340 18.803 −1.302 1.00 27.64 ATOM 1297 NE ARG A 466 20.588 19.665 −0.400 1.00 26.47 ATOM 1298 CZ ARG A 466 21.076 20.728 0.234 1.00 24.01 ATOM 1299 NH1 ARG A 466 22.341 21.082 0.092 1.00 20.35 ATOM 1300 NH2 ARG A 466 20.266 21.477 0.969 1.00 25.10 ATOM 1301 C ARG A 466 22.613 16.155 −4.681 1.00 32.20 ATOM 1302 O ARG A 466 21.981 15.542 −5.543 1.00 34.80 ATOM 1303 N SER A 467 23.852 15.835 −4.343 1.00 31.72 ATOM 1304 CA SER A 467 24.512 14.700 −4.961 1.00 29.23 ATOM 1305 CB SER A 467 25.915 14.497 −4.373 1.00 30.36 ATOM 1306 OG SER A 467 26.750 15.613 −4.579 1.00 34.62 ATOM 1307 C SER A 467 23.705 13.442 −4.680 1.00 29.79 ATOM 1308 O SER A 467 23.050 13.327 −3.653 1.00 27.96 ATOM 1309 N TRP A 468 23.760 12.504 −5.610 1.00 27.51 ATOM 1310 CA TRP A 468 23.114 11.203 −5.476 1.00 27.13 ATOM 1311 CB TRP A 468 23.703 10.431 −4.286 1.00 30.38 ATOM 1312 CG TRP A 468 25.196 10.650 −4.109 1.00 33.34 ATOM 1313 CD2 TRP A 468 26.241 10.375 −5.068 1.00 34.52 ATOM 1314 CE2 TRP A 468 27.453 10.853 −4.510 1.00 34.97 ATOM 1315 CE3 TRP A 468 26.271 9.778 −6.345 1.00 33.99 ATOM 1316 CD1 TRP A 468 25.807 11.246 −3.043 1.00 35.05 ATOM 1317 NE1 TRP A 468 27.152 11.376 −3.278 1.00 35.95 ATOM 1318 CZ2 TRP A 468 28.688 10.755 −5.182 1.00 32.97 ATOM 1319 CZ3 TRP A 468 27.494 9.677 −7.012 1.00 29.70 ATOM 1320 CH2 TRP A 468 28.686 10.167 −6.425 1.00 34.34 ATOM 1321 C TRP A 468 21.602 11.121 −5.472 1.00 27.07 ATOM 1322 O TRP A 468 21.042 10.084 −5.105 1.00 29.52 ATOM 1323 N LEU A 469 20.921 12.190 −5.874 1.00 27.42 ATOM 1324 CA LEU A 469 19.456 12.139 −5.945 1.00 30.07 ATOM 1325 CB LEU A 469 18.910 13.539 −6.099 1.00 28.28 ATOM 1326 CG LEU A 469 18.898 14.353 −4.824 1.00 24.65 ATOM 1327 CD1 LEU A 469 18.463 15.758 −5.160 1.00 26.09 ATOM 1328 CD2 LEU A 469 17.929 13.704 −3.867 1.00 20.08 ATOM 1329 C LEU A 469 19.028 11.294 −7.155 1.00 33.83 ATOM 1330 O LEU A 469 19.735 11.285 −8.146 1.00 39.39 ATOM 1331 N GLN A 470 17.916 10.564 −7.077 1.00 34.69 ATOM 1332 CA GLN A 470 17.463 9.757 −8.224 1.00 39.38 ATOM 1333 CB GLN A 470 16.832 8.443 −7.779 1.00 40.10 ATOM 1334 CG GLN A 470 17.796 7.485 −7.120 1.00 50.51 ATOM 1335 CD GLN A 470 17.111 6.245 −6.571 1.00 55.73 ATOM 1336 OE1 GLN A 470 15.993 5.911 −6.964 1.00 57.73 ATOM 1337 NE2 GLN A 470 17.776 5.565 −5.643 1.00 58.82 ATOM 1338 C GLN A 470 16.444 10.524 −9.050 1.00 40.91 ATOM 1339 O GLN A 470 16.619 10.727 −10.250 1.00 42.98 ATOM 1340 N GLU A 471 15.383 10.960 −8.386 1.00 40.83 ATOM 1341 CA GLU A 471 14.308 11.720 −9.013 1.00 40.88 ATOM 1342 CB GLU A 471 13.001 11.447 −8.269 1.00 40.93 ATOM 1343 CG GLU A 471 12.699 9.972 −8.077 1.00 48.61 ATOM 1344 CD GLU A 471 11.560 9.737 −7.098 1.00 53.74 ATOM 1345 OE1 GLU A 471 10.392 10.051 −7.438 1.00 52.66 ATOM 1346 OE2 GLU A 471 11.841 9.243 −5.981 1.00 59.20 ATOM 1347 C GLU A 471 14.588 13.235 −9.046 1.00 41.53 ATOM 1348 O GLU A 471 13.780 14.027 −8.551 1.00 42.72 ATOM 1349 N LYS A 472 15.707 13.634 −9.657 1.00 41.50 ATOM 1350 CA LYS A 472 16.086 15.044 −9.750 1.00 41.09 ATOM 1351 CB LYS A 472 17.332 15.198 −10.614 1.00 38.72 ATOM 1352 CG LYS A 472 18.592 14.669 −9.971 1.00 43.30 ATOM 1353 CD LYS A 472 19.731 15.695 −10.033 1.00 46.29 ATOM 1354 CE LYS A 472 20.679 15.517 −8.831 1.00 50.44 ATOM 1355 NZ LYS A 472 21.892 16.398 −8.804 1.00 46.13 ATOM 1356 C LYS A 472 14.978 15.941 −10.287 1.00 43.56 ATOM 1357 O LYS A 472 14.628 16.963 −9.689 1.00 43.75 ATOM 1358 N VAL A 473 14.399 15.511 −11.402 1.00 46.51 ATOM 1359 CA VAL A 473 13.326 16.236 −12.084 1.00 43.88 ATOM 1360 CB VAL A 473 12.963 15.516 −13.416 1.00 49.53 ATOM 1361 CG1 VAL A 473 11.696 16.128 −14.040 1.00 51.00 ATOM 1362 CG2 VAL A 473 14.155 15.611 −14.395 1.00 49.56 ATOM 1363 C VAL A 473 12.076 16.466 −11.235 1.00 37.01 ATOM 1364 O VAL A 473 11.536 17.572 −11.212 1.00 33.80 ATOM 1365 N LYS A 474 11.609 15.415 −10.570 1.00 36.39 ATOM 1366 CA LYS A 474 10.440 15.508 −9.695 1.00 36.93 ATOM 1367 CB LYS A 474 10.084 14.126 −9.147 1.00 35.35 ATOM 1368 CG LYS A 474 8.886 14.077 −8.218 1.00 38.41 ATOM 1369 CD LYS A 474 8.579 12.626 −7.848 1.00 46.48 ATOM 1370 CE LYS A 474 7.746 12.480 −6.569 1.00 53.40 ATOM 1371 NZ LYS A 474 6.298 12.790 −6.709 1.00 57.86 ATOM 1372 C LYS A 474 10.713 16.495 −8.537 1.00 37.36 ATOM 1373 O LYS A 474 9.887 17.359 −8.250 1.00 36.85 ATOM 1374 N ILE A 475 11.897 16.422 −7.927 1.00 37.31 ATOM 1375 CA ILE A 475 12.231 17.328 −6.820 1.00 37.61 ATOM 1376 CB ILE A 475 13.535 16.887 −6.067 1.00 35.04 ATOM 1377 CG2 ILE A 475 13.834 17.877 −4.931 1.00 34.59 ATOM 1378 CG1 ILE A 475 13.368 15.464 −5.488 1.00 27.42 ATOM 1379 CD1 ILE A 475 14.680 14.711 −5.243 1.00 18.44 ATOM 1380 C ILE A 475 12.349 18.766 −7.352 1.00 40.05 ATOM 1381 O ILE A 475 11.882 19.727 −6.721 1.00 38.84 ATOM 1382 N GLU A 476 12.913 18.896 −8.550 1.00 41.69 ATOM 1383 CA GLU A 476 13.066 20.184 −9.207 1.00 43.30 ATOM 1384 CB GLU A 476 13.755 19.984 −10.552 1.00 48.95 ATOM 1385 CG GLU A 476 13.732 21.196 −11.464 1.00 62.73 ATOM 1386 CD GLU A 476 14.355 22.442 −10.846 1.00 70.08 ATOM 1387 OE1 GLU A 476 15.464 22.338 −10.274 1.00 76.26 ATOM 1388 OE2 GLU A 476 13.741 23.532 −10.947 1.00 75.60 ATOM 1389 C GLU A 476 11.705 20.850 −9.413 1.00 42.70 ATOM 1390 O GLU A 476 11.547 22.050 −9.183 1.00 38.37 ATOM 1391 N LYS A 477 10.724 20.066 −9.854 1.00 41.95 ATOM 1392 CA LYS A 477 9.379 20.580 −10.072 1.00 45.24 ATOM 1393 CB LYS A 477 8.461 19.496 −10.643 1.00 49.85 ATOM 1394 CG LYS A 477 8.971 18.848 −11.905 1.00 59.55 ATOM 1395 CD LYS A 477 9.158 19.879 −12.984 1.00 69.14 ATOM 1396 CE LYS A 477 9.721 19.258 −14.243 1.00 75.50 ATOM 1397 NZ LYS A 477 9.631 20.220 −15.382 1.00 82.60 ATOM 1398 C LYS A 477 8.798 21.075 −8.753 1.00 45.20 ATOM 1399 O LYS A 477 8.303 22.207 −8.668 1.00 44.88 ATOM 1400 N LEU A 478 8.850 20.216 −7.728 1.00 42.02 ATOM 1401 CA LEU A 478 8.339 20.575 −6.403 1.00 39.03 ATOM 1402 CB LEU A 478 8.506 19.411 −5.419 1.00 38.50 ATOM 1403 CG LEU A 478 7.562 18.213 −5.609 1.00 38.77 ATOM 1404 CD1 LEU A 478 7.919 17.062 −4.658 1.00 40.42 ATOM 1405 CD2 LEU A 478 6.126 18.653 −5.389 1.00 36.80 ATOM 1406 C LEU A 478 9.020 21.856 −5.875 1.00 37.92 ATOM 1407 O LEU A 478 8.332 22.767 −5.399 1.00 37.49 ATOM 1408 N GLN A 479 10.344 21.963 −6.057 1.00 37.80 ATOM 1409 CA GLN A 479 11.083 23.144 −5.607 1.00 38.11 ATOM 1410 CB GLN A 479 12.610 22.987 −5.772 1.00 36.91 ATOM 1411 CG GLN A 479 13.425 24.177 −5.189 1.00 40.17 ATOM 1412 CD GLN A 479 14.938 24.122 −5.452 1.00 42.02 ATOM 1413 OE1 GLN A 479 15.411 23.469 −6.392 1.00 48.01 ATOM 1414 NE2 GLN A 479 15.702 24.820 −4.616 1.00 46.19 ATOM 1415 C GLN A 479 10.589 24.379 −6.343 1.00 39.25 ATOM 1416 O GLN A 479 10.392 25.426 −5.718 1.00 42.08 ATOM 1417 N GLN A 480 10.348 24.251 −7.650 1.00 39.34 ATOM 1418 CA GLN A 480 9.855 25.371 −8.460 1.00 43.07 ATOM 1419 CB GLN A 480 9.547 24.917 −9.894 1.00 51.07 ATOM 1420 CG GLN A 480 10.733 24.407 −10.707 1.00 64.44 ATOM 1421 CD GLN A 480 10.291 23.533 −11.889 1.00 73.00 ATOM 1422 OE1 GLN A 480 9.132 23.582 −12.310 1.00 75.34 ATOM 1423 NE2 GLN A 480 11.211 22.732 −12.425 1.00 72.93 ATOM 1424 C GLN A 480 8.591 25.987 −7.853 1.00 37.24 ATOM 1425 O GLN A 480 8.499 27.198 −7.658 1.00 35.48 ATOM 1426 N LYS A 481 7.620 25.139 −7.545 1.00 35.17 ATOM 1427 CA LYS A 481 6.381 25.614 −6.957 1.00 37.36 ATOM 1428 CB LYS A 481 5.397 24.470 −6.801 1.00 41.26 ATOM 1429 CG LYS A 481 4.877 23.975 −8.112 1.00 49.18 ATOM 1430 CD LYS A 481 3.683 23.105 −7.907 1.00 59.24 ATOM 1431 CE LYS A 481 2.989 22.839 −9.229 1.00 68.40 ATOM 1432 NZ LYS A 481 1.798 21.950 −9.050 1.00 76.15 ATOM 1433 C LYS A 481 6.599 26.317 −5.628 1.00 37.73 ATOM 1434 O LYS A 481 5.976 27.353 −5.360 1.00 35.72 ATOM 1435 N ILE A 482 7.486 25.748 −4.806 1.00 38.76 ATOM 1436 CA ILE A 482 7.831 26.299 −3.494 1.00 36.16 ATOM 1437 CB ILE A 482 8.817 25.381 −2.705 1.00 32.89 ATOM 1438 CG2 ILE A 482 9.404 26.130 −1.514 1.00 34.55 ATOM 1439 CG1 ILE A 482 8.112 24.093 −2.234 1.00 28.40 ATOM 1440 CD1 ILE A 482 9.070 23.005 −1.769 1.00 24.86 ATOM 1441 C ILE A 482 8.447 27.681 −3.639 1.00 35.37 ATOM 1442 O ILE A 482 8.152 28.579 −2.864 1.00 36.18 ATOM 1443 N GLN A 483 9.256 27.862 −4.668 1.00 38.47 ATOM 1444 CA GLN A 483 9.867 29.164 −4.892 1.00 39.76 ATOM 1445 CB GLN A 483 10.932 29.071 −5.950 1.00 40.59 ATOM 1446 CG GLN A 483 11.712 30.342 −6.053 1.00 49.20 ATOM 1447 CD GLN A 483 12.711 30.296 −7.192 1.00 58.50 ATOM 1448 OE1 GLN A 483 12.820 29.303 −7.861 1.00 65.68 ATOM 1449 NE2 GLN A 483 13.440 31.368 −7.409 1.00 65.23 ATOM 1450 C GLN A 483 8.843 30.239 −5.284 1.00 40.84 ATOM 1451 O GLN A 483 8.969 31.422 −4.923 1.00 38.66 ATOM 1452 N LEU A 484 7.802 29.820 −6.002 1.00 39.88 ATOM 1453 CA LEU A 484 6.754 30.730 −6.439 1.00 42.14 ATOM 1454 CB LEU A 484 5.812 30.033 −7.416 1.00 45.74 ATOM 1455 CG LEU A 484 6.403 29.624 −8.765 1.00 48.71 ATOM 1456 CD1 LEU A 484 5.337 28.943 −9.615 1.00 48.20 ATOM 1457 CD2 LEU A 484 6.966 30.856 −9.472 1.00 50.22 ATOM 1458 C LEU A 484 5.957 31.241 −5.252 1.00 42.55 ATOM 1459 O LEU A 484 5.622 32.424 −5.181 1.00 42.64 ATOM 1460 N ALA A 485 5.626 30.329 −4.338 1.00 43.56 ATOM 1461 CA ALA A 485 4.872 30.672 −3.128 1.00 40.84 ATOM 1462 CB ALA A 485 4.350 29.403 −2.449 1.00 41.40 ATOM 1463 C ALA A 485 5.729 31.497 −2.162 1.00 37.33 ATOM 1464 O ALA A 485 5.204 32.298 −1.388 1.00 37.52 ATOM 1465 N LEU A 486 7.047 31.293 −2.215 1.00 35.33 ATOM 1466 CA LEU A 486 7.979 32.036 −1.380 1.00 38.02 ATOM 1467 CB LEU A 486 9.371 31.401 −1.395 1.00 32.53 ATOM 1468 CG LEU A 486 10.451 32.287 −0.758 1.00 33.21 ATOM 1469 CD1 LEU A 486 10.176 32.478 0.723 1.00 32.27 ATOM 1470 CD2 LEU A 486 11.818 31.693 −0.965 1.00 31.01 ATOM 1471 C LEU A 486 8.049 33.457 −1.942 1.00 42.86 ATOM 1472 O LEU A 486 8.077 34.446 −1.190 1.00 44.35 ATOM 1473 N GLN A 487 8.070 33.545 −3.271 1.00 44.64 ATOM 1474 CA GLN A 487 8.112 34.813 −3.998 1.00 47.16 ATOM 1475 CB GLN A 487 8.145 34.502 −5.486 1.00 51.86 ATOM 1476 CG GLN A 487 9.000 35.408 −6.310 1.00 61.53 ATOM 1477 CD GLN A 487 9.486 34.714 −7.571 1.00 65.93 ATOM 1478 OE1 GLN A 487 9.083 33.587 −7.865 1.00 66.76 ATOM 1479 NE2 GLN A 487 10.369 35.373 −8.311 1.00 70.60 ATOM 1480 C GLN A 487 6.823 35.579 −3.655 1.00 47.05 ATOM 1481 O GLN A 487 6.844 36.754 −3.307 1.00 45.17 ATOM 1482 N HIS A 488 5.702 34.874 −3.741 1.00 47.07 ATOM 1483 CA HIS A 488 4.387 35.405 −3.423 1.00 48.67 ATOM 1484 CB HIS A 488 3.374 34.280 −3.608 1.00 51.60 ATOM 1485 CG HIS A 488 2.095 34.484 −2.868 1.00 59.15 ATOM 1486 CD2 HIS A 488 1.638 33.939 −1.715 1.00 62.57 ATOM 1487 ND1 HIS A 488 1.097 35.317 −3.322 1.00 63.45 ATOM 1488 CE1 HIS A 488 0.074 35.272 −2.485 1.00 64.94 ATOM 1489 NE2 HIS A 488 0.378 34.444 −1.500 1.00 65.61 ATOM 1490 C HIS A 488 4.334 35.962 −1.986 1.00 49.05 ATOM 1491 O HIS A 488 3.925 37.097 −1.757 1.00 48.47 ATOM 1492 N VAL A 489 4.755 35.154 −1.021 1.00 48.07 ATOM 1493 CA VAL A 489 4.763 35.571 0.381 1.00 45.44 ATOM 1494 CB VAL A 489 5.220 34.401 1.302 1.00 46.07 ATOM 1495 CG1 VAL A 489 5.592 34.911 2.692 1.00 44.85 ATOM 1496 CG2 VAL A 489 4.115 33.372 1.409 1.00 41.76 ATOM 1497 C VAL A 489 5.682 36.773 0.580 1.00 43.28 ATOM 1498 O VAL A 489 5.319 37.741 1.229 1.00 41.87 ATOM 1499 N LEU A 490 6.866 36.706 −0.006 1.00 44.44 ATOM 1500 CA LEU A 490 7.865 37.763 0.103 1.00 49.79 ATOM 1501 CB LEU A 490 9.075 37.410 −0.766 1.00 50.68 ATOM 1502 CG LEU A 490 10.389 36.884 −0.181 1.00 54.00 ATOM 1503 CD1 LEU A 490 10.223 36.100 1.115 1.00 54.10 ATOM 1504 CD2 LEU A 490 11.034 36.035 −1.241 1.00 54.17 ATOM 1505 C LEU A 490 7.338 39.122 −0.310 1.00 52.92 ATOM 1506 O LEU A 490 7.224 40.037 0.498 1.00 50.59 ATOM 1507 N GLN A 491 7.014 39.243 −1.587 1.00 60.06 ATOM 1508 CA GLN A 491 6.513 40.494 −2.107 1.00 66.69 ATOM 1509 CB GLN A 491 6.560 40.523 −3.638 1.00 72.00 ATOM 1510 CG GLN A 491 6.078 39.292 −4.373 1.00 75.89 ATOM 1511 CD GLN A 491 6.340 39.394 −5.862 1.00 79.38 ATOM 1512 OE1 GLN A 491 7.133 40.231 −6.302 1.00 82.32 ATOM 1513 NE2 GLN A 491 5.672 38.554 −6.647 1.00 81.82 ATOM 1514 C GLN A 491 5.144 40.863 −1.555 1.00 68.27 ATOM 1515 O GLN A 491 4.820 42.045 −1.433 1.00 69.36 ATOM 1516 N LYS A 492 4.360 39.863 −1.168 1.00 69.33 ATOM 1517 CA LYS A 492 3.055 40.123 −0.581 1.00 70.57 ATOM 1518 CB LYS A 492 2.464 38.825 −0.036 1.00 63.87 ATOM 1519 CG LYS A 492 1.419 39.011 1.021 1.00 55.18 ATOM 1520 CD LYS A 492 0.936 37.684 1.518 1.00 50.15 ATOM 1521 CE LYS A 492 0.170 36.960 0.445 1.00 47.92 ATOM 1522 NZ LYS A 492 −0.429 35.700 0.955 1.00 49.79 ATOM 1523 C LYS A 492 3.258 41.101 0.561 1.00 76.10 ATOM 1524 O LYS A 492 2.447 41.991 0.778 1.00 78.57 ATOM 1525 N ASN A 493 4.387 40.955 1.245 1.00 83.09 ATOM 1526 CA ASN A 493 4.724 41.795 2.380 1.00 90.65 ATOM 1527 CB ASN A 493 5.326 40.936 3.510 1.00 91.76 ATOM 1528 CG ASN A 493 4.413 39.791 3.960 1.00 91.33 ATOM 1529 OD1 ASN A 493 3.483 39.989 4.743 1.00 90.45 ATOM 1530 ND2 ASN A 493 4.727 38.576 3.525 1.00 90.60 ATOM 1531 C ASN A 493 5.703 42.929 2.053 1.00 96.54 ATOM 1532 O ASN A 493 5.445 44.097 2.361 1.00 97.40 ATOM 1533 N HIS A 494 6.815 42.593 1.401 1.00 104.63 ATOM 1534 CA HIS A 494 7.847 43.592 1.111 1.00 112.99 ATOM 1535 CB HIS A 494 9.092 43.302 1.972 1.00 118.20 ATOM 1536 CG HIS A 494 8.776 42.865 3.375 1.00 123.22 ATOM 1537 CD2 HIS A 494 8.606 41.630 3.906 1.00 124.65 ATOM 1538 ND1 HIS A 494 8.580 43.754 4.409 1.00 125.31 ATOM 1539 CE1 HIS A 494 8.306 43.087 5.517 1.00 125.71 ATOM 1540 NE2 HIS A 494 8.314 41.796 5.238 1.00 124.45 ATOM 1541 C HIS A 494 8.283 43.810 −0.343 1.00 115.21 ATOM 1542 O HIS A 494 9.414 43.476 −0.719 1.00 113.88 ATOM 1543 N ARG A 495 7.411 44.411 −1.150 1.00 118.74 ATOM 1544 CA ARG A 495 7.771 44.693 −2.539 1.00 123.08 ATOM 1545 CB ARG A 495 6.532 44.895 −3.411 1.00 124.19 ATOM 1546 CG ARG A 495 5.922 43.611 −3.923 1.00 125.95 ATOM 1547 CD ARG A 495 4.905 43.869 −5.022 1.00 128.86 ATOM 1548 NE ARG A 495 4.097 42.688 −5.336 1.00 130.65 ATOM 1549 CZ ARG A 495 2.771 42.700 −5.469 1.00 131.44 ATOM 1550 NH1 ARG A 495 2.089 43.829 −5.316 1.00 132.26 ATOM 1551 NH2 ARG A 495 2.122 41.580 −5.755 1.00 132.05 ATOM 1552 C ARG A 495 8.677 45.927 −2.632 1.00 124.82 ATOM 1553 O ARG A 495 9.086 46.332 −3.723 1.00 125.80 ATOM 1554 N GLU A 496 8.979 46.520 −1.479 1.00 125.27 ATOM 1555 CA GLU A 496 9.840 47.694 −1.403 1.00 125.62 ATOM 1556 CB GLU A 496 10.086 48.053 0.060 1.00 125.24 ATOM 1557 CG GLU A 496 10.364 46.856 0.953 1.00 125.43 ATOM 1558 CD GLU A 496 10.161 47.175 2.414 1.00 127.70 ATOM 1559 OE1 GLU A 496 11.014 47.880 2.992 1.00 129.15 ATOM 1560 OE2 GLU A 496 9.137 46.733 2.981 1.00 127.94 ATOM 1561 C GLU A 496 11.162 47.439 −2.117 1.00 126.43 ATOM 1562 O GLU A 496 11.731 48.346 −2.723 1.00 127.96 ATOM 1563 N ASP A 497 11.635 46.195 −2.047 1.00 126.16 ATOM 1564 CA ASP A 497 12.886 45.790 −2.693 1.00 124.22 ATOM 1565 CB ASP A 497 14.036 45.643 −1.669 1.00 124.95 ATOM 1566 CG ASP A 497 13.719 46.260 −0.317 1.00 125.55 ATOM 1567 OD1 ASP A 497 13.970 47.468 −0.132 1.00 125.55 ATOM 1568 OD2 ASP A 497 13.221 45.530 0.565 1.00 126.80 ATOM 1569 C ASP A 497 12.646 44.446 −3.392 1.00 121.48 ATOM 1570 O ASP A 497 11.524 44.142 −3.807 1.00 121.28 ATOM 1571 N GLY A 498 13.711 43.655 −3.527 1.00 118.36 ATOM 1572 CA GLY A 498 13.637 42.337 −4.142 1.00 112.17 ATOM 1573 C GLY A 498 14.617 41.465 −3.374 1.00 106.96 ATOM 1574 O GLY A 498 15.677 41.104 −3.889 1.00 107.39 ATOM 1575 N ILE A 499 14.253 41.158 −2.128 1.00 100.38 ATOM 1576 CA ILE A 499 15.058 40.378 −1.187 1.00 90.88 ATOM 1577 CB ILE A 499 14.545 40.644 0.259 1.00 89.37 ATOM 1578 CG2 ILE A 499 14.172 39.362 0.988 1.00 88.94 ATOM 1579 CG1 ILE A 499 15.573 41.483 1.013 1.00 88.59 ATOM 1580 CD1 ILE A 499 16.015 42.736 0.254 1.00 88.83 ATOM 1581 C ILE A 499 15.254 38.885 −1.469 1.00 85.97 ATOM 1582 O ILE A 499 16.120 38.243 −0.872 1.00 81.39 ATOM 1583 N LEU A 500 14.482 38.353 −2.412 1.00 82.32 ATOM 1584 CA LEU A 500 14.572 36.945 −2.784 1.00 79.33 ATOM 1585 CB LEU A 500 13.593 36.610 −3.926 1.00 75.45 ATOM 1586 CG LEU A 500 13.480 35.160 −4.427 1.00 72.35 ATOM 1587 CD1 LEU A 500 13.020 34.209 −3.345 1.00 70.46 ATOM 1588 CD2 LEU A 500 12.509 35.104 −5.569 1.00 74.01 ATOM 1589 C LEU A 500 15.994 36.594 −3.191 1.00 78.86 ATOM 1590 O LEU A 500 16.443 35.483 −2.943 1.00 80.08 ATOM 1591 N THR A 501 16.709 37.548 −3.786 1.00 78.15 ATOM 1592 CA THR A 501 18.085 37.316 −4.224 1.00 79.02 ATOM 1593 CB THR A 501 18.654 38.487 −5.065 1.00 82.06 ATOM 1594 OG1 THR A 501 18.870 39.635 −4.225 1.00 84.30 ATOM 1595 CG2 THR A 501 17.708 38.834 −6.214 1.00 83.64 ATOM 1596 C THR A 501 18.935 37.193 −2.988 1.00 77.23 ATOM 1597 O THR A 501 19.694 36.236 −2.831 1.00 77.82 ATOM 1598 N LYS A 502 18.776 38.185 −2.117 1.00 74.83 ATOM 1599 CA LYS A 502 19.478 38.276 −0.847 1.00 72.92 ATOM 1600 CB LYS A 502 18.834 39.402 −0.025 1.00 79.85 ATOM 1601 CG LYS A 502 19.726 40.108 0.995 1.00 85.84 ATOM 1602 CD LYS A 502 18.937 41.231 1.690 1.00 89.85 ATOM 1603 CE LYS A 502 19.744 41.963 2.764 1.00 94.60 ATOM 1604 NZ LYS A 502 18.918 42.984 3.487 1.00 95.90 ATOM 1605 C LYS A 502 19.282 36.922 −0.158 1.00 66.91 ATOM 1606 O LYS A 502 20.227 36.332 0.360 1.00 65.72 ATOM 1607 N LEU A 503 18.060 36.409 −0.267 1.00 59.20 ATOM 1608 CA LEU A 503 17.662 35.134 0.306 1.00 52.88 ATOM 1609 CB LEU A 503 16.158 34.971 0.156 1.00 47.50 ATOM 1610 CG LEU A 503 15.466 34.377 1.365 1.00 49.58 ATOM 1611 CD1 LEU A 503 16.066 34.928 2.664 1.00 46.78 ATOM 1612 CD2 LEU A 503 13.990 34.688 1.270 1.00 51.22 ATOM 1613 C LEU A 503 18.374 33.938 −0.314 1.00 51.55 ATOM 1614 O LEU A 503 19.200 33.301 0.334 1.00 49.38 ATOM 1615 N ILE A 504 18.087 33.645 −1.579 1.00 50.92 ATOM 1616 CA ILE A 504 18.715 32.499 −2.231 1.00 51.60 ATOM 1617 CB ILE A 504 18.054 32.153 −3.588 1.00 55.42 ATOM 1618 CG2 ILE A 504 16.718 31.464 −3.360 1.00 52.28 ATOM 1619 CG1 ILE A 504 17.860 33.415 −4.418 1.00 59.46 ATOM 1620 CD1 ILE A 504 16.623 33.368 −5.320 1.00 67.68 ATOM 1621 C ILE A 504 20.233 32.598 −2.336 1.00 49.75 ATOM 1622 O ILE A 504 20.917 31.593 −2.485 1.00 50.38 ATOM 1623 N CYS A 505 20.773 33.798 −2.192 1.00 48.02 ATOM 1624 CA CYS A 505 22.221 33.974 −2.220 1.00 49.31 ATOM 1625 CB CYS A 505 22.557 35.465 −2.457 1.00 58.96 ATOM 1626 SG CYS A 505 23.762 36.304 −1.354 1.00 77.11 ATOM 1627 C CYS A 505 22.791 33.433 −0.891 1.00 46.24 ATOM 1628 O CYS A 505 23.956 33.014 −0.803 1.00 41.30 ATOM 1629 N LYS A 506 21.939 33.398 0.131 1.00 40.06 ATOM 1630 CA LYS A 506 22.336 32.890 1.425 1.00 37.35 ATOM 1631 CB LYS A 506 21.286 33.221 2.481 1.00 40.11 ATOM 1632 CG LYS A 506 20.957 34.686 2.596 1.00 43.49 ATOM 1633 CD LYS A 506 22.217 35.514 2.611 1.00 51.34 ATOM 1634 CE LYS A 506 22.343 36.269 3.891 1.00 55.65 ATOM 1635 NZ LYS A 506 22.139 35.376 5.071 1.00 63.77 ATOM 1636 C LYS A 506 22.466 31.389 1.309 1.00 36.27 ATOM 1637 O LYS A 506 23.267 30.786 2.005 1.00 40.04 ATOM 1638 N VAL A 507 21.692 30.784 0.417 1.00 32.90 ATOM 1639 CA VAL A 507 21.735 29.341 0.227 1.00 35.32 ATOM 1640 CB VAL A 507 20.809 28.932 −0.926 1.00 39.14 ATOM 1641 CG1 VAL A 507 20.872 27.438 −1.155 1.00 41.89 ATOM 1642 CG2 VAL A 507 19.382 29.364 −0.630 1.00 35.73 ATOM 1643 C VAL A 507 23.146 28.782 −0.016 1.00 35.01 ATOM 1644 O VAL A 507 23.447 27.642 0.318 1.00 36.47 ATOM 1645 N SER A 508 24.009 29.584 −0.616 1.00 36.29 ATOM 1646 CA SER A 508 25.372 29.159 −0.886 1.00 37.66 ATOM 1647 CB SER A 508 25.996 30.084 −1.941 1.00 38.93 ATOM 1648 OG SER A 508 27.309 29.693 −2.294 1.00 45.66 ATOM 1649 C SER A 508 26.192 29.172 0.420 1.00 37.79 ATOM 1650 O SER A 508 27.026 28.280 0.647 1.00 37.44 ATOM 1651 N THR A 509 25.949 30.178 1.267 1.00 35.49 ATOM 1652 CA THR A 509 26.627 30.326 2.553 1.00 32.31 ATOM 1653 CB THR A 509 26.250 31.644 3.236 1.00 35.78 ATOM 1654 OG1 THR A 509 26.405 32.720 2.305 1.00 42.43 ATOM 1655 CG2 THR A 509 27.157 31.895 4.437 1.00 35.82 ATOM 1656 C THR A 509 26.231 29.187 3.469 1.00 28.28 ATOM 1657 O THR A 509 27.065 28.665 4.178 1.00 32.41 ATOM 1658 N LEU A 510 24.958 28.812 3.452 1.00 28.16 ATOM 1659 CA LEU A 510 24.452 27.696 4.249 1.00 29.00 ATOM 1660 CB LEU A 510 22.994 27.394 3.885 1.00 26.48 ATOM 1661 CG LEU A 510 21.819 28.079 4.571 1.00 29.80 ATOM 1662 CD1 LEU A 510 20.544 27.623 3.907 1.00 28.25 ATOM 1663 CD2 LEU A 510 21.793 27.717 6.063 1.00 30.36 ATOM 1664 C LEU A 510 25.267 26.437 3.969 1.00 32.43 ATOM 1665 O LEU A 510 25.639 25.698 4.885 1.00 32.33 ATOM 1666 N ARG A 511 25.524 26.194 2.685 1.00 31.40 ATOM 1667 CA ARG A 511 26.272 25.027 2.233 1.00 28.94 ATOM 1668 CB ARG A 511 26.170 24.909 0.706 1.00 34.59 ATOM 1669 CG ARG A 511 24.716 24.741 0.261 1.00 34.26 ATOM 1670 CD ARG A 511 24.547 24.611 −1.225 1.00 36.35 ATOM 1671 NE ARG A 511 23.192 24.185 −1.556 1.00 31.13 ATOM 1672 CZ ARG A 511 22.887 23.356 −2.545 1.00 31.68 ATOM 1673 NH1 ARG A 511 23.839 22.856 −3.324 1.00 32.54 ATOM 1674 NH2 ARG A 511 21.628 23.004 −2.730 1.00 27.68 ATOM 1675 C ARG A 511 27.710 25.049 2.695 1.00 26.34 ATOM 1676 O ARG A 511 28.270 24.011 3.015 1.00 28.74 ATOM 1677 N ALA A 512 28.314 26.235 2.693 1.00 25.39 ATOM 1678 CA ALA A 512 29.687 26.409 3.161 1.00 24.68 ATOM 1679 CB ALA A 512 30.157 27.796 2.830 1.00 22.96 ATOM 1680 C ALA A 512 29.732 26.195 4.691 1.00 27.69 ATOM 1681 O ALA A 512 30.622 25.518 5.231 1.00 27.18 ATOM 1652 N LEU A 513 28.773 26.814 5.373 1 00 27 .15 ATOM 1683 CA LEU A 513 28.638 26.708 6.815 1.00 26.64 ATOM 1684 CB LEU A 513 27.427 27.528 7.256 1.00 24.45 ATOM 1685 CG LEU A 513 27.228 27.696 8.758 1.00 28.40 ATOM 1686 CD1 LEU A 513 28.492 28.230 9.403 1.00 25.85 ATOM 1687 CD2 LEU A 513 26.053 28.607 9.013 1.00 30.72 ATOM 1688 C LEU A 513 28.490 25.209 7.192 1.00 29.10 ATOM 1689 O LEU A 513 29.259 24.683 8.008 1.00 31.91 ATOM 1690 N CYS A 514 27.543 24.512 6.566 1.00 26.57 ATOM 1691 CA CYS A 514 27.351 23.104 6.851 1.00 26.98 ATOM 1692 CB CYS A 514 26.025 22.614 6.269 1.00 25.74 ATOM 1693 SG CYS A 514 24.579 23.438 7.009 1.00 30.96 ATOM 1694 C CYS A 514 28.538 22.250 6.404 1.00 28.07 ATOM 1695 O CYS A 514 28.764 21.161 6.931 1.00 27.30 ATOM 1696 N GLY A 515 29.298 22.741 5.431 1.00 29.78 ATOM 1697 CA GLY A 515 30.477 22.027 4.980 1.00 29.40 ATOM 1698 C GLY A 515 31.570 22.004 6.040 1.00 30.10 ATOM 1699 O GLY A 515 32.190 20.965 6.266 1.00 30.71 ATOM 1700 N ARG A 516 31.810 23.142 6.693 1.00 33.97 ATOM 1701 CA ARG A 516 32.811 23.217 7.748 1.00 34.03 ATOM 1702 CB ARG A 516 33.065 24.652 8.178 1.00 37.07 ATOM 1703 CG ARG A 516 33.921 25.429 7.198 1.00 52.01 ATOM 1704 CD ARG A 516 34.465 26.715 7.807 1.00 56.98 ATOM 1705 NE ARG A 516 35.467 26.438 8.836 1.00 61.64 ATOM 1706 CZ ARG A 516 35.927 27.342 9.699 1.00 62.65 ATOM 1707 NH1 ARG A 516 35.466 28.590 9.665 1.00 61.40 ATOM 1708 NH2 ARG A 516 36.879 27.005 10.566 1.00 60.38 ATOM 1709 C ARG A 516 32.380 22.395 8.947 1.00 33.89 ATOM 1710 O ARG A 516 33.227 21.847 9.634 1.00 33.31 ATOM 1711 N HIS A 517 31.075 22.322 9.215 1.00 33.19 ATOM 1712 CA HIS A 517 30.616 21.517 10.337 1.00 34.62 ATOM 1713 CB HIS A 517 29.085 21.466 10.440 1.00 34.29 ATOM 1714 CG HIS A 517 28.576 20.462 11.440 1.00 33.44 ATOM 1715 CD2 HIS A 517 28.646 20.433 12.793 1.00 31.33 ATOM 1716 ND1 HIS A 517 27.909 19.311 11.072 1.00 28.67 ATOM 1717 CE1 HIS A 517 27.589 18.619 12.151 1.00 27.08 ATOM 1718 NE2 HIS A 517 28.027 19.279 13.208 1.00 28.43 ATOM 1719 C HIS A 517 31.147 20.107 10.127 1.00 36.73 ATOM 1720 O HIS A 517 31.825 19.567 10.994 1.00 34.74 ATOM 1721 N THR A 518 30.884 19.541 8.950 1.00 36.75 ATOM 1722 CA THR A 518 31.343 18.192 8.662 1.00 36.81 ATOM 1723 CB THR A 518 30.692 17.620 7.406 1.00 35.05 ATOM 1724 OG1 THR A 518 29.327 17.303 7.688 1.00 37.15 ATOM 1725 CG2 THR A 518 31.382 16.346 6.980 1.00 38.73 ATOM 1726 C THR A 518 32.862 18.100 8.608 1.00 37.39 ATOM 1727 O THR A 518 33.430 17.077 8.962 1.00 42.45 ATOM 1728 N GLU A 519 33.531 19.175 8.220 1.00 38.67 ATOM 1729 CA GLU A 519 34.990 19.166 8.196 1.00 43.58 ATOM 1730 CB GLU A 519 35.516 20.438 7.500 1.00 54.27 ATOM 1731 CG GLU A 519 35.261 20.537 5.964 1.00 63.20 ATOM 1732 CD GLU A 519 35.380 21.975 5.406 1.00 65.12 ATOM 1733 OE1 GLU A 519 34.782 22.258 4.342 1.00 66.49 ATOM 1734 OE2 GLU A 519 36.053 22.826 6.035 1.00 67.73 ATOM 1735 C GLU A 519 35.516 19.099 9.649 1.00 42.46 ATOM 1736 O GLU A 519 36.470 18.382 9.959 1.00 39.74 ATOM 1737 N LYS A 520 34.857 19.843 10.535 1.00 41.75 ATOM 1738 CA LYS A 520 35.222 19.895 11.945 1.00 37.07 ATOM 1739 CB LYS A 520 34.481 21.049 12.651 1.00 41.10 ATOM 1740 CG LYS A 520 34.939 22.467 12.235 1.00 44.66 ATOM 1741 CD LYS A 520 36.383 22.748 12.670 1.00 53.92 ATOM 1742 CE LYS A 520 37.078 23.819 11.819 1.00 56.95 ATOM 1743 NZ LYS A 520 37.313 23.411 10.388 1.00 63.31 ATOM 1744 C LYS A 520 34.911 18.560 12.618 1.00 34.80 ATOM 1745 O LYS A 520 35.770 17.983 13.278 1.00 34.89 ATOM 1746 N LEU A 521 33.703 18.051 12.394 1.00 33.45 ATOM 1747 CA LEU A 521 33.270 16.782 12.956 1.00 33.31 ATOM 1748 CB LEU A 521 31.839 16.460 12.526 1.00 26.37 ATOM 1749 CG LEU A 521 31.268 15.095 12.905 1.00 24.78 ATOM 1750 CD1 LEU A 521 31.380 14.865 14.394 1.00 29.22 ATOM 1751 CD2 LEU A 521 29.832 15.021 12.520 1.00 24.85 ATOM 1752 C LEU A 521 34.214 15.633 12.601 1.00 38.43 ATOM 1753 O LEU A 521 34.564 14.843 13.477 1.00 38.10 ATOM 1754 N MET A 522 34.694 15.581 11.356 1.00 39.97 ATOM 1755 CA MET A 522 35.601 14.507 10.947 1.00 41.97 ATOM 1756 CB MET A 522 35.725 14.431 9.426 1.00 48.01 ATOM 1757 CG MET A 522 34.430 14.035 8.707 1.00 58.55 ATOM 1758 SD MET A 522 33.355 12.804 9.548 1.00 67.62 ATOM 1759 CE MET A 522 34.455 11.351 9.732 1.00 65.55 ATOM 1760 C MET A 522 36.982 14.574 11.596 1.00 40.03 ATOM 1761 O MET A 522 37.578 13.539 11.900 1.00 37.83 ATOM 1762 N ALA A 523 37.497 15.782 11.798 1.00 37.94 ATOM 1763 CA ALA A 523 38.790 15.936 12.452 1.00 39.72 ATOM 1764 CB ALA A 523 39.272 17.353 12.304 1.00 45.50 ATOM 1765 C ALA A 523 38.640 15.587 13.938 1.00 41.81 ATOM 1766 O ALA A 523 39.523 14.997 14.547 1.00 44.06 ATOM 1767 N PHE A 524 37.509 15.971 14.519 1.00 41.49 ATOM 1768 CA PHE A 524 37.238 15.674 15.915 1.00 39.19 ATOM 1769 CB PHE A 524 35.923 16.334 16.360 1.00 35.12 ATOM 1770 CG PHE A 524 35.511 15.998 17.781 1.00 30.17 ATOM 1771 CD1 PHE A 524 35.968 16.762 18.852 1.00 28.22 ATOM 1772 CD2 PHE A 524 34.644 14.924 18.040 1.00 26.69 ATOM 1773 CE1 PHE A 524 35.569 16.465 20.166 1.00 25.14 ATOM 1774 CE2 PHE A 524 34.240 14.620 19.341 1.00 27.45 ATOM 1775 CZ PHE A 524 34.709 15.398 20.408 1.00 25.33 ATOM 1776 C PHE A 524 37.151 14.157 16.093 1.00 38.05 ATOM 1777 O PHE A 524 37.788 13.602 16.989 1.00 39.38 ATOM 1778 N LYS A 525 36.370 13.494 15.240 1.00 33.74 ATOM 1779 CA LYS A 525 36.188 12.053 15.336 1.00 32.28 ATOM 1780 CB LYS A 525 35.150 11.566 14.341 1.00 32.43 ATOM 1781 CG LYS A 525 35.058 10.061 14.265 1.00 32.27 ATOM 1782 CD LYS A 525 34.049 9.588 13.234 1.00 39.70 ATOM 1783 CE LYS A 525 34.182 8.085 13.027 1.00 43.60 ATOM 1784 NZ LYS A 525 33.052 7.475 12.274 1.00 52.36 ATOM 1785 C LYS A 525 37.486 11.292 15.141 1.00 37.02 ATOM 1786 O LYS A 525 37.572 10.113 15.458 1.00 38.38 ATOM 1787 N ALA A 526 38.514 11.972 14.651 1.00 38.57 ATOM 1788 CA ALA A 526 39.796 11.312 14.442 1.00 42.31 ATOM 1789 CB ALA A 526 40.639 12.098 13.429 1.00 42.02 ATOM 1790 C ALA A 526 40.523 11.230 15.774 1.00 43.27 ATOM 1791 O ALA A 526 41.174 10.226 16.091 1.00 43.91 ATOM 1792 N ILE A 527 40.348 12.293 16.555 1.00 41.76 ATOM 1793 CA ILE A 527 40.961 12.455 17.866 1.00 40.21 ATOM 1794 CB ILE A 527 41.127 13.946 18.166 1.00 40.67 ATOM 1795 CG2 ILE A 527 41.824 14.145 19.503 1.00 42.82 ATOM 1796 CG1 ILE A 527 41.897 14.612 17.026 1.00 39.18 ATOM 1797 CD1 ILE A 527 41.864 16.128 17.066 1.00 37.42 ATOM 1798 C ILE A 527 40.195 11.786 19.015 1.00 38.56 ATOM 1799 O ILE A 527 40.800 11.309 19.974 1.00 38.98 ATOM 1800 N TYR A 528 38.871 11.727 18.900 1.00 34.57 ATOM 1801 CA TYR A 528 38.023 11.135 19.930 1.00 31.38 ATOM 1802 CB TYR A 528 37.209 12.229 20.645 1.00 31.31 ATOM 1803 CG TYR A 528 38.046 13.379 21.159 1.00 34.92 ATOM 1804 CD1 TYR A 528 38.337 14.471 20.345 1.00 34.80 ATOM 1805 CE1 TYR A 528 39.157 15.513 20.789 1.00 39.08 ATOM 1806 CD2 TYR A 528 38.592 13.355 22.442 1.00 34.45 ATOM 1807 CE2 TYR A 528 39.417 14.394 22.895 1.00 37.74 ATOM 1808 CZ TYR A 528 39.695 15.468 22.062 1.00 39.56 ATOM 1809 OH TYR A 528 40.520 16.489 22.489 1.00 45.36 ATOM 1810 C TYR A 528 37.066 10.113 19.333 1.00 32.21 ATOM 1811 O TYR A 528 35.843 10.289 19.388 1.00 35.37 ATOM 1812 N PRO A 529 37.601 9.010 18.777 1.00 32.25 ATOM 1813 CD PRO A 529 39.034 8.705 18.673 1.00 29.41 ATOM 1814 CA PRO A 529 36.809 7.939 18.160 1.00 30.81 ATOM 1815 CB PRO A 529 37.875 6.895 17.822 1.00 30.02 ATOM 1816 CG PRO A 529 39.061 7.703 17.564 1.00 29.92 ATOM 1817 C PRO A 529 35.706 7.331 19.040 1.00 33.28 ATOM 1818 O PRO A 529 34.553 7.201 18.606 1.00 32.51 ATOM 1819 N ASP A 530 36.066 6.953 20.272 1.00 35.37 ATOM 1820 CA ASP A 530 35.110 6.338 21.195 1.00 35.88 ATOM 1821 CB ASP A 530 35.831 5.563 22.293 1.00 46.50 ATOM 1822 CG ASP A 530 36.564 4.341 21.758 1.00 58.80 ATOM 1823 OD1 ASP A 530 36.010 3.219 21.852 1.00 64.43 ATOM 1824 OD2 ASP A 530 37.697 4.503 21.240 1.00 63.77 ATOM 1825 C ASP A 530 34.127 7.309 21.799 1.00 29.27 ATOM 1826 O ASP A 530 33.037 6.909 22.221 1.00 29.58 ATOM 1827 N ILE A 531 34.525 8.577 21.892 1.00 30.58 ATOM 1828 CA ILE A 531 33.629 9.593 22.426 1.00 29.77 ATOM 1829 CB ILE A 531 34.302 10.998 22.576 1.00 35.01 ATOM 1830 CG2 ILE A 531 33.230 12.090 22.817 1.00 33.87 ATOM 1831 CG1 ILE A 531 35.247 10.998 23.781 1.00 36.43 ATOM 1832 CD1 ILE A 531 34.549 10.604 25.107 1.00 36.43 ATOM 1833 C ILE A 531 32.500 9.673 21.440 1.00 29.02 ATOM 1834 O ILE A 531 31.344 9.560 21.819 1.00 33.33 ATOM 1835 N VAL A 532 32.841 9.787 20.158 1.00 29.79 ATOM 1836 CA VAL A 532 31.814 9.857 19.129 1.00 25.98 ATOM 1837 CB VAL A 532 32.446 10.141 17.746 1.00 27.17 ATOM 1838 CG1 VAL A 532 31.376 10.244 16.699 1.00 26.57 ATOM 1839 CG2 VAL A 532 33.246 11.437 17.788 1.00 23.54 ATOM 1840 C VAL A 532 30.984 8.567 19.111 1.00 22.88 ATOM 1841 O VAL A 532 29.765 8.596 19.258 1.00 25.44 ATOM 1842 N ARG A 533 31.662 7.429 19.048 1.00 24.52 ATOM 1843 CA ARG A 533 30.980 6.136 18.997 1.00 23.99 ATOM 1844 CB ARG A 533 32.028 5.030 18.941 1.00 28.41 ATOM 1845 CG ARG A 533 31.444 3.657 18.777 1.00 37.43 ATOM 1846 CD ARG A 533 32.551 2.627 18.668 1.00 45.29 ATOM 1847 WE ARG A 533 32.255 1.490 19.528 1.00 51.73 ATOM 1848 CZ ARG A 533 32.897 1.228 20.658 1.00 55.49 ATOM 1849 NH1 ARG A 533 33.899 2.010 21.052 1.00 51.92 ATOM 1850 NH2 ARG A 533 32.459 0.254 21.445 1.00 59.77 ATOM 1851 C ARG A 533 30.024 5.861 20.136 1.00 24.93 ATOM 1852 O ARG A 533 28.866 5.504 19.935 1.00 24.06 ATOM 1853 N LEU A 534 30.519 6.093 21.348 1.00 30.94 ATOM 1854 CA LEU A 534 29.778 5.846 22.582 1.00 26.49 ATOM 1855 CB LEU A 534 30.773 5.408 23.658 1.00 28.50 ATOM 1856 CG LEU A 534 31.461 4.072 23.339 1.00 28.71 ATOM 1857 CD1 LEU A 534 32.692 3.806 24.193 1.00 29.88 ATOM 1858 CD2 LEU A 534 30.436 2.985 23.497 1.00 29.34 ATOM 1859 C LEU A 534 28.877 6.956 23.118 1.00 24.89 ATOM 1860 O LEU A 534 27.803 6.669 23.649 1.00 24.01 ATOM 1861 N HIS A 535 29.234 8.214 22.875 1.00 25.63 ATOM 1862 CA HIS A 535 28.458 9.317 23.439 1.00 27.16 ATOM 1863 CB HIS A 535 29.358 10.074 24.423 1.00 26.58 ATOM 1864 CG HIS A 535 30.001 9.174 25.430 1.00 25.50 ATOM 1865 CD2 HIS A 535 31.245 8.641 25.487 1.00 25.11 ATOM 1866 ND1 HIS A 535 29.302 8.631 26.487 1.00 26.41 ATOM 1867 CE1 HIS A 535 30.086 7.802 27.151 1.00 24.19 ATOM 1868 NE2 HIS A 535 31.270 7.790 26.564 1.00 26.77 ATOM 1869 C HIS A 535 27.669 10.284 22.553 1.00 28.58 ATOM 1870 O HIS A 535 26.881 11.073 23.082 1.00 27.81 ATOM 1871 N PHE A 536 27.851 10.228 21.226 1.00 33.00 ATOM 1872 CA PHE A 536 27.092 11.108 20.313 1.00 31.11 ATOM 1873 CB PHE A 536 27.895 11.401 19.043 1.00 29.90 ATOM 1874 CG PHE A 536 28.915 12.512 19.192 1.00 29.99 ATOM 1875 CD1 PHE A 536 29.678 12.643 20.337 1.00 24.61 ATOM 1876 CD2 PHE A 536 29.132 13.406 18.153 1.00 25.96 ATOM 1877 CE1 PHE A 536 30.644 13.642 20.439 1.00 23.54 ATOM 1878 CE2 PHE A 536 30.095 14.406 18.256 1.00 24.50 ATOM 1879 CZ PHE A 536 30.849 14.523 19.394 1.00 24.21 ATOM 1880 C PHE A 536 25.713 10.487 19.970 1.00 31.08 ATOM 1881 O PHE A 536 25.581 9.259 19.956 1.00 34.36 ATOM 1882 N PRO A 537 24.664 11.321 19.756 1.00 27.00 ATOM 1883 CD PRO A 537 24.632 12.793 19.845 1.00 25.60 ATOM 1884 CA PRO A 537 23.335 10.795 19.432 1.00 25.30 ATOM 1885 CB PRO A 537 22.501 12.068 19.256 1.00 23.10 ATOM 1886 CG PRO A 537 23.189 13.062 20.157 1.00 22.43 ATOM 1887 C PRO A 537 23.392 9.975 18.128 1.00 30.48 ATOM 1888 O PRO A 537 24.122 10.336 17.185 1.00 28.64 ATOM 1889 N PRO A 538 22.690 8.823 18.091 1.00 31.20 ATOM 1890 CD PRO A 538 22.017 8.173 19.227 1.00 28.91 ATOM 1891 CA PRO A 538 22.654 7.946 16.908 1.00 32.16 ATOM 1892 CB PRO A 538 21.592 6.931 17.293 1.00 29.35 ATOM 1893 CG PRO A 538 21.911 6.731 18.759 1.00 28.32 ATOM 1894 C PRO A 538 22.311 8.708 15.623 1.00 32.64 ATOM 1895 O PRO A 538 23.086 8.680 14.669 1.00 30.42 ATOM 1896 N LEU A 539 21.207 9.460 15.652 1.00 34.18 ATOM 1897 CA LEU A 539 20.773 10.273 14.510 1.00 30.02 ATOM 1898 CB LEU A 539 19.512 11.069 14.895 1.00 29.47 ATOM 1899 CG LEU A 539 18.858 11.924 13.802 1.00 29.66 ATOM 1900 CD1 LEU A 539 18.592 11.029 12.608 1.00 31.73 ATOM 1901 CD2 LEU A 539 17.583 12.604 14.267 1.00 25.29 ATOM 1902 C LEU A 539 21.887 11.215 14.009 1.00 29.19 ATOM 1903 O LEU A 539 22.131 11.326 12.816 1.00 30.25 ATOM 1904 N TYR A 540 22.581 11.877 14.925 1.00 25.32 ATOM 1905 CA TYR A 540 23.643 12.778 14.546 1.00 22.42 ATOM 1906 CB TYR A 540 24.280 13.355 15.791 1.00 21.19 ATOM 1907 CG TYR A 540 25.343 14.387 15.535 1.00 17.26 ATOM 1908 CD1 TYR A 540 25.016 15.733 15.400 1.00 17.30 ATOM 1909 CE1 TYR A 540 25.982 16.676 15.216 1.00 12.79 ATOM 1910 CD2 TYR A 540 26.680 14.028 15.464 1.00 19.93 ATOM 1911 CE2 TYR A 540 27.657 14.976 15.268 1.00 20.13 ATOM 1912 CZ TYR A 540 27.294 16.299 15.150 1.00 13.88 ATOM 1913 OH TYR A 540 28.276 17.244 14.997 1.00 21.75 ATOM 1914 C TYR A 540 24.708 12.009 13.780 1.00 32.70 ATOM 1915 O TYR A 540 25.296 12.508 12.811 1.00 34.57 ATOM 1916 N LYS A 541 25.008 10.802 14.244 1.00 35.66 ATOM 1917 CA LYS A 541 26.029 9.999 13.574 1.00 36.65 ATOM 1918 CB LYS A 541 26.482 8.874 14.497 1.00 32.71 ATOM 1919 CG LYS A 541 27.219 9.383 15.714 1.00 31.67 ATOM 1920 CD LYS A 541 27.712 8.227 16.528 1.00 26.84 ATOM 1921 CE LYS A 541 26.561 7.418 17.035 1.00 22.56 ATOM 1922 NZ LYS A 541 27.091 6.148 17.574 1.00 31.19 ATOM 1923 C LYS A 541 25.563 9.467 12.204 1.00 32.35 ATOM 1924 O LYS A 541 26.324 9.441 11.250 1.00 34.75 ATOM 1925 N GLU A 542 24.298 9.069 12.126 1.00 32.04 ATOM 1926 CA GLU A 542 23.726 8.570 10.888 1.00 35.69 ATOM 1927 CB GLU A 542 22.316 8.074 11.129 1.00 38.46 ATOM 1928 CG GLU A 542 22.269 6.772 11.888 1.00 52.51 ATOM 1929 CD GLU A 542 20.882 6.443 12.403 1.00 59.88 ATOM 1930 OE1 GLU A 542 20.795 5.892 13.531 1.00 65.14 ATOM 1931 OE2 GLU A 542 19.889 6.732 11.684 1.00 59.01 ATOM 1932 C GLU A 542 23.661 9.668 9.855 1.00 36.75 ATOM 1933 O GLU A 542 23.668 9.393 8.666 1.00 39.22 ATOM 1934 N LEU A 543 23.557 10.913 10.312 1.00 35.21 ATOM 1935 CA LEU A 543 23.449 12.047 9.407 1.00 33.98 ATOM 1936 CB LEU A 543 22.549 13.145 9.990 1.00 31.70 ATOM 1937 CG LEU A 543 21.045 12.927 10.118 1.00 34.06 ATOM 1938 CD1 LEU A 543 20.457 14.088 10.891 1.00 35.24 ATOM 1939 CD2 LEU A 543 20.388 12.826 8.761 1.00 35.42 ATOM 1940 C LEU A 543 24.731 12.702 8.959 1.00 32.29 ATOM 1941 O LEU A 543 24.776 13.231 7.859 1.00 39.03 ATOM 1942 N PHE A 544 25.781 12.651 9.762 1.00 29.28 ATOM 1943 CA PHE A 544 26.997 13.354 9.389 1.00 29.14 ATOM 1944 CB PHE A 544 27.203 14.561 10.330 1.00 32.64 ATOM 1945 CG PHE A 544 25.969 15.425 10.528 1.00 32.31 ATOM 1946 CD1 PHE A 544 25.295 15.431 11.746 1.00 27.53 ATOM 1947 CD2 PHE A 544 25.491 16.247 9.501 1.00 32.38 ATOM 1948 CE1 PHE A 544 24.165 16.239 11.943 1.00 26.56 ATOM 1949 CE2 PHE A 544 24.354 17.065 9.690 1.00 29.30 ATOM 1950 CZ PHE A 544 23.694 17.057 10.914 1.00 30.03 ATOM 1951 C PHE A 544 28.269 12.505 9.356 1.00 33.29 ATOM 1952 O PHE A 544 28.193 11.266 9.571 1.00 36.40 ATOM 1953 OXT PHE A 544 29.349 13.102 9.110 1.00 34.60 ATOM 1954 O1 HOH V 1 19.571 24.015 22.830 1.00 11.92 ATOM 1955 O1 HOH V 2 12.600 24.091 16.912 1.00 16.18 ATOM 1956 O1 HOH V 3 14.052 22.894 14.638 1.00 22.41 ATOM 1957 O1 HOH V 4 28.663 16.841 27.507 1.00 23.15 ATOM 1958 O1 HOH V 5 26.725 9.526 26.728 1.00 24.50 ATOM 1959 O1 HOH V 6 18.179 21.587 21.082 1.00 24.52 ATOM 1960 O1 HOH V 7 34.584 18.654 31.591 1.00 24.62 ATOM 1961 O1 HOH V 8 38.207 8.705 22.227 1.00 25.07 ATOM 1962 O1 HOH V 9 18.077 19.002 0.819 1.00 25.07 ATOM 1963 O1 HOH V 10 17.420 26.679 24.799 1.00 25.52 ATOM 1964 O1 HOH V 11 11.110 25.828 9.180 1.00 25.56 ATOM 1965 O1 HOH V 12 25.371 34.354 26.992 1.00 25.89 ATOM 1966 O1 HOH V 13 35.321 27.213 19.620 1.00 25.99 ATOM 1967 O1 HOH V 14 18.045 26.166 21.645 1.00 26.14 ATOM 1968 O1 HOH V 15 19.454 10.080 17.919 1.00 26.31 ATOM 1969 O1 HOH V 16 37.357 26.490 13.415 1.00 26.89 ATOM 1970 O1 HOH V 17 11.508 26.772 18.302 1.00 27.31 ATOM 1971 O1 HOH V 18 15.147 25.780 21.426 1.00 27.73 ATOM 1972 O1 HOH V 19 26.400 37.545 37.765 1.00 27.84 ATOM 1973 O1 HOH V 20 24.927 38.184 32.702 1.00 28.88 ATOM 1974 O1 HOH V 21 22.535 18.724 7.093 1.00 29.31 ATOM 1975 O1 HOH V 22 19.050 8.455 −3.987 1.00 29.80 ATOM 1976 O1 HOH V 23 20.732 38.540 24.291 1.00 30.07 ATOM 1977 O1 HOH V 24 14.054 28.783 15.745 1.00 31.20 ATOM 1978 O1 HOH V 25 25.356 15.005 28.051 1.00 31.83 ATOM 1979 O1 HOH V 26 33.279 26.348 25.938 1.00 32.16 ATOM 1980 O1 HOH V 27 14.590 28.615 28.744 1.00 32.70 ATOM 1981 O1 HOH V 28 4.102 35.198 9.164 1.00 32.70 ATOM 1982 O1 HOH V 29 13.577 30.615 29.768 1.00 32.70 ATOM 1983 O1 HOH V 30 28.564 37.851 14.236 1.00 32.76 ATOM 1984 O1 HOH V 31 22.927 14.143 0.962 1.00 33.39 ATOM 1985 O1 HOH V 32 27.550 38.081 22.254 1.00 33.51 ATOM 1986 O1 HOH V 33 4.343 30.099 9.792 1.00 33.68 ATOM 1987 O1 HOH V 34 13.758 27.478 19.451 1.00 33.73 ATOM 1988 O1 HOH V 35 31.045 36.851 16.729 1.00 33.87 ATOM 1989 O1 HOH V 36 19.213 14.762 21.135 1.00 33.94 ATOM 1990 O1 HOH V 37 30.260 38.889 20.375 1.00 34.05 ATOM 1991 O1 HOH V 38 21.211 20.354 29.122 1.00 34.10 ATOM 1992 O1 HOH V 39 32.966 5.622 27.344 1.00 34.62 ATOM 1993 O1 HOH V 40 26.116 6.668 20.629 1.00 35.56 ATOM 1994 O1 HOH V 41 −1.516 28.517 7.655 1.00 35.63 ATOM 1995 O1 HOH V 42 34.189 32.470 17.850 1.00 35.68 ATOM 1996 O1 HOH V 43 24.220 21.292 3.001 1.00 35.74 ATOM 1997 O1 HOH V 44 5.910 27.836 16.119 1.00 36.07 ATOM 1998 O1 HOH V 45 26.026 15.360 5.513 1.00 36.54 ATOM 1999 O1 HOH V 46 24.021 14.774 −1.204 1.00 36.65 ATOM 2000 O1 HOH V 47 20.363 26.930 31.179 1.00 36.70 ATOM 2001 O1 HOH V 48 35.665 32.840 10.425 1.00 36.70 ATOM 2002 O1 HOH V 49 26.360 37.660 34.946 1.00 36.83 ATOM 2003 O1 HOH V 50 25.128 17.207 −1.881 1.00 36.96 ATOM 2004 O1 HOH V 51 24.114 21.504 30.329 1.00 37.03 ATOM 2005 O1 HOH V 52 15.366 43.743 10.778 1.00 37.39 ATOM 2006 O1 HOH V 53 30.933 6.183 15.530 1.00 37.82 ATOM 2007 O1 HOH V 54 4.304 36.868 5.949 1.00 38.21 ATOM 2008 O1 HOH V 55 14.763 35.710 19.412 1.00 39.01 ATOM 2009 O1 HOH V 56 1.357 20.195 9.921 1.00 39.03 ATOM 2010 O1 HOH V 57 13.913 23.892 19.724 1.00 39.09 ATOM 2011 O1 HOH V 58 12.354 12.577 −11.744 1.00 39.57 ATOM 2012 O1 HOH V 59 19.367 4.873 15.945 1.00 39.60 ATOM 2013 O1 HOH V 60 28.823 27.044 −1.138 1.00 39.87 ATOM 2014 O1 HOH V 61 24.086 5.629 14.333 1.00 39.92 ATOM 2015 O1 HOH V 62 6.227 36.542 12.153 1.00 39.94 ATOM 2016 O1 HOH V 63 25.257 19.031 30.271 1.00 40.01 ATOM 2017 O1 HOH V 64 33.091 35.051 17.676 1.00 40.07 ATOM 2018 O1 HOH V 65 33.832 31.154 20.549 1.00 40.37 ATOM 2019 O1 HOH V 66 40.477 15.296 9.510 1.00 41.20 ATOM 2020 O1 HOH V 67 23.525 9.325 −8.918 1.00 41.87 ATOM 2021 O1 HOH V 68 18.624 25.089 −4.128 1.00 42.15 ATOM 2022 O1 HOH V 69 24.673 39.002 −1.542 1.00 42.21 ATOM 2023 O1 HOH V 70 25.134 15.085 2.723 1.00 42.21 ATOM 2024 O1 HOH V 71 10.336 29.797 26.075 1.00 42.37 ATOM 2025 O1 HOH V 72 16.798 18.655 −11.711 1.00 42.43 ATOM 2026 O1 HOH V 73 −2.391 33.028 0.604 1.00 42.69 ATOM 2027 O1 HOH V 74 7.033 20.764 20.270 1.00 43.01 ATOM 2028 O1 HOH V 75 27.375 26.586 32.414 1.00 43.08 ATOM 2029 O1 HOH V 76 24.651 12.458 27.335 1.00 43.14 ATOM 2030 O1 HOH V 77 21.223 24.850 0.260 1.00 43.31 ATOM 2031 O1 HOH V 78 13.059 10.272 13.532 1.00 43.63 ATOM 2032 O1 HOH V 79 27.284 19.103 8.210 1.00 44.00 ATOM 2033 O1 HOH V 80 34.897 34.595 21.757 1.00 44.35 ATOM 2034 O1 HOH V 81 19.496 24.289 −1.468 1.00 44.41 ATOM 2035 O1 HOH V 82 26.589 22.429 32.257 1.00 44.58 ATOM 2036 O1 HOH V 83 41.875 11.753 22.776 1.00 44.72 ATOM 2037 O1 HOH V 84 24.041 16.824 29.300 1.00 44.91 ATOM 2038 O1 HOH V 85 39.182 23.600 24.591 1.00 45.03 ATOM 2039 O1 HOH V 86 16.711 29.367 31.469 1.00 45.22 ATOM 2040 O1 HOH V 87 26.474 37.247 27.330 1.00 45.42 ATOM 2041 O1 HOH V 88 10.580 10.952 7.001 1.00 45.46 ATOM 2042 O1 HOH V 89 17.919 17.134 23.482 1.00 45.53 ATOM 2043 O1 HOH V 90 22.700 27.169 33.013 1.00 45.86 ATOM 2044 O1 HOH V 91 20.218 40.609 29.025 1.00 46.30 ATOM 2045 O1 HOH V 92 21.955 40.569 26.103 1.00 46.31 ATOM 2046 O1 HOH V 93 5.333 26.234 18.852 1.00 46.91 ATOM 2047 O1 HOH V 94 6.403 18.038 15.920 1.00 47.12 ATOM 2048 O1 HOH V 95 37.307 11.015 10.807 1.00 47.31 ATOM 2049 O1 HOH V 96 11.338 13.464 13.985 1.00 47.96 ATOM 2050 O1 HOH V 97 10.441 37.707 30.346 1.00 48.02 ATOM 2051 O1 HOH V 98 30.888 36.428 14.084 1.00 48.48 ATOM 2052 O1 HOH V 99 27.882 17.980 29.841 1.00 48.50 ATOM 2053 O1 HOH V 100 33.749 37.917 8.734 1.00 48.51 ATOM 2054 O1 HOH V 101 18.379 27.870 33.046 1.00 48.64 ATOM 2055 O1 HOH V 102 35.449 31.668 8.141 1.00 48.94 ATOM 2056 O1 HOH V 103 29.164 17.601 3.576 1.00 49.29 ATOM 2057 O1 HOH V 104 33.653 32.899 6.888 1.00 49.36 ATOM 2058 O1 HOH V 105 42.507 15.827 13.475 1.00 49.69 ATOM 2059 O1 HOH V 106 37.222 20.712 33.061 1.00 49.71 ATOM 2060 O1 HOH V 107 19.173 42.140 26.556 1.00 49.87 ATOM 2061 O1 HOH V 108 −1.128 28.133 10.338 1.00 50.07 ATOM 2062 O1 HOH V 109 13.605 40.750 25.634 1.00 50.16 ATOM 2063 O1 HOH V 110 −1.457 28.059 −4.001 1.00 50.19 ATOM 2064 O1 HOH V 111 −0.092 31.118 6.416 1.00 50.25 ATOM 2065 O1 HOH V 112 3.374 39.612 −3.935 1.00 50.31 ATOM 2066 O1 HOH V 113 32.127 18.267 32.763 1.00 50.37 ATOM 2067 O1 HOH V 114 18.258 23.101 26.041 1.00 50.51 ATOM 2068 O1 HOH V 115 26.516 26.089 −3.694 1.00 50.63 ATOM 2069 O1 HOH V 116 13.352 17.048 19.784 1.00 50.83 ATOM 2070 O1 HOH V 117 10.647 6.108 12.167 1.00 50.93 ATOM 2071 O1 HOH V 118 26.146 17.547 1.891 1.00 50.94 ATOM 2072 O1 HOH V 119 15.203 21.870 20.133 1.00 50.98 ATOM 2073 O1 HOH V 120 32.029 18.786 4.116 1.00 51.10 ATOM 2074 O1 HOH V 121 22.114 18.269 27.109 1.00 51.46 ATOM 2075 O1 HOH V 122 25.668 18.396 5.657 1.00 51.52 ATOM 2076 O1 HOH V 123 41.989 18.102 20.145 1.00 51.77 ATOM 2077 O1 HOH V 124 36.078 5.753 14.297 1.00 52.16 ATOM 2078 O1 HOH V 125 −4.191 23.385 −0.546 1.00 52.19 ATOM 2079 O1 HOH V 126 38.840 23.465 28.263 1.00 52.44 ATOM 2080 O1 HOH V 127 17.889 40.107 16.024 1.00 52.46 ATOM 2081 O1 HOH V 128 10.480 31.213 29.646 1.00 52.47 ATOM 2082 O1 HOH V 129 11.041 40.539 4.064 1.00 52.63 ATOM 2083 O1 HOH V 130 25.662 37.407 30.124 1.00 52.65 ATOM 2084 O1 HOH V 131 37.583 19.513 14.379 1.00 52.79 ATOM 2085 O1 HOH V 132 31.355 36.654 28.009 1.00 52.82 ATOM 2086 O1 HOH V 133 24.495 25.685 32.162 1.00 52.92 ATOM 2087 O1 HOH V 134 29.710 0.923 19.113 1.00 52.92 ATOM 2088 O1 HOH V 135 17.608 9.016 9.185 1.00 52.96 ATOM 2089 O1 HOH V 136 24.883 4.742 16.973 1.00 53.32 ATOM 2090 O1 HOH V 137 29.325 41.144 15.563 1.00 54.00 ATOM 2091 O1 HOH V 138 8.148 32.691 27.089 1.00 54.14 ATOM 2092 O1 HOH V 139 25.869 44.302 17.088 1.00 54.60 ATOM 2093 O1 HOH V 140 31.180 24.098 0.471 1.00 54.96 ATOM 2094 O1 HOH V 141 32.092 39.604 16.380 1.00 55.48 ATOM 2095 O1 HOH V 142 20.031 28.982 35.641 1.00 55.95 ATOM 2096 O1 HOH V 143 19.537 17.716 26.209 1.00 56.58 ATOM 2097 O1 HOH V 144 3.004 26.615 21.765 1.00 56.65 ATOM 2098 O1 HOH V 145 3.566 13.601 10.033 1.00 56.98 ATOM 2099 O1 HOH V 146 16.090 48.803 −0.839 1.00 57.02 ATOM 2100 O1 HOH V 147 41.521 30.957 16.321 1.00 57.24 ATOM 2101 O1 HOH V 148 21.322 6.331 6.002 1.00 57.58 ATOM 2102 O1 HOH V 149 9.375 39.538 12.218 1.00 57.59 ATOM 2103 O1 HOH V 150 15.176 39.661 18.686 1.00 58.07 ATOM 2104 O1 HOH V 151 20.363 24.179 31.362 1.00 58.21 ATOM 2105 O1 HOH V 152 14.157 40.583 21.313 1.00 58.26 ATOM 2106 O1 HOH V 153 13.420 36.512 16.363 1.00 58.51 ATOM 2107 O1 HOH V 154 1.911 36.126 4.549 1.00 58.55 ATOM 2108 O1 HOH V 155 16.108 6.884 12.075 1.00 58.70 ATOM 2109 O1 HOH V 156 −4.815 29.631 −4.704 1.00 58.74 ATOM 2110 O1 HOH V 157 17.728 4.118 0.882 1.00 59.17 ATOM 2111 O1 HOH V 158 11.034 33.423 31.437 1.00 59.38 ATOM 2112 O1 HOH V 159 39.277 19.752 9.565 1.00 59.80 ATOM 2113 O1 HOH V 160 20.830 23.224 −9.945 1.00 59.89 ATOM 2114 O1 HOH V 161 29.709 18.612 31.510 1.00 60.09 ATOM 2115 O1 HOH V 162 27.074 2.621 20.642 1.00 60.12 ATOM 2116 O1 HOH V 163 5.858 22.161 −4.489 1.00 60.19 ATOM 2117 O1 HOH V 164 15.034 44.034 5.590 1.00 60.39 ATOM 2118 O1 HOH V 165 33.009 22.978 33.387 1.00 60.43 ATOM 2119 O1 HOH V 166 2.030 21.719 −4.397 1.00 60.59 ATOM 2120 O1 HOH V 167 3.774 21.532 3.731 1.00 60.68 ATOM 2121 O1 HOH V 168 28.412 13.665 −7.177 1.00 60.83 ATOM 2122 O1 HOH V 169 39.061 22.162 31.337 1.00 61.22 ATOM 2123 O1 HOH V 170 30.385 11.086 11.347 1.00 61.45 ATOM 2124 O1 HOH V 171 38.929 11.728 26.423 1.00 61.62 ATOM 2125 O1 HOH V 172 9.596 6.343 −6.409 1.00 61.85 ATOM 2126 O1 HOH V 173 27.960 21.516 2.108 1.00 61.90 ATOM 2127 O1 HOH V 174 4.313 13.515 −0.097 1.00 62.15 ATOM 2128 O1 HOH V 175 −4.186 27.811 7.260 1.00 62.60 ATOM 2129 O1 HOH V 176 10.940 41.489 27.508 1.00 63.29 ATOM 2130 O1 HOH V 177 24.701 19.822 −1.623 1.00 63.64 ATOM 2131 O1 HOH V 178 42.644 18.535 10.330 1.00 63.68 ATOM 2132 O1 HOH V 179 1.986 36.706 26.540 1.00 63.68 ATOM 2133 O1 HOH V 180 22.345 47.189 18.548 1.00 64.72 ATOM 2134 O1 HOH V 181 7.492 6.994 1.249 1.00 64.77 ATOM 2135 O1 HOH V 182 29.348 37.819 26.783 1.00 64.90 ATOM 2136 O1 HOH V 183 39.883 20.258 25.832 1.00 65.05 ATOM 2137 O1 HOH V 184 33.197 24.977 3.656 1.00 65.28 ATOM 2138 O1 HOH V 185 1.167 34.045 3.205 1.00 65.41 ATOM 2139 O1 HOH V 186 36.275 32.735 23.649 1.00 65.48 ATOM 2140 O1 HOH V 187 −2.787 30.904 −0.828 1.00 65.58 ATOM 2141 O1 HOH V 188 6.538 23.682 −10.695 1.00 66.34 ATOM 2142 O1 HOH V 189 10.682 8.724 11.380 1.00 66.87 ATOM 2143 O1 HOH V 190 14.198 8.869 −12.442 1.00 67.21 ATOM 2144 O1 HOH V 191 −2.267 38.672 −2.479 1.00 67.22 ATOM 2145 O1 HOH V 192 29.224 8.950 12.107 1.00 67.30 ATOM 2146 O1 HOH V 193 11.819 8.883 6.281 1.00 67.62 ATOM 2147 O1 HOH V 194 38.489 16.915 8.462 1.00 68.36 ATOM 2148 O1 HOH V 195 33.987 7.482 15.967 1.00 68.84 ATOM 2149 O1 HOH V 196 4.892 34.328 −7.351 1.00 68.88 ATOM 2150 O1 HOH V 197 39.056 27.510 8.823 1.00 68.92 ATOM 2151 O1 HOH V 198 9.884 6.802 3.712 1.00 69.08 ATOM 2152 O1 HOH V 199 37.843 34.495 12.256 1.00 69.20 ATOM 2153 O1 HOH V 200 34.349 36.343 19.667 1.00 69.76 ATOM 2154 O1 HOH V 201 38.474 1.028 20.411 1.00 70.03 ATOM 2155 O1 HOH V 202 27.053 38.768 25.134 1.00 70.09 ATOM 2156 O1 HOH V 203 28.267 37.799 29.494 1.00 70.65 ATOM 2157 O1 HOH V 204 25.427 35.915 1.694 1.00 71.85 ATOM 2158 O1 HOH V 205 18.375 3.341 9.734 1.00 72.08 ATOM 2159 O1 HOH V 206 29.055 24.527 −1.260 1.00 72.11 ATOM 2160 O1 HOH V 207 15.436 3.667 −5.477 1.00 72.50 ATOM 2161 O1 HOH V 208 2.845 25.343 17.594 1.00 72.71 ATOM 2162 O1 HOH V 209 31.127 39.615 33.793 1.00 74.83 ATOM 2163 O1 HOH V 210 15.559 12.402 −12.936 1.00 75.70 ATOM 2164 O1 HOH V 211 40.158 26.133 22.103 1.00 76.15 ATOM 2165 O1 HOH V 212 3.811 32.891 15.563 1.00 77.51 ATOM 2166 O1 HOH V 213 21.251 45.356 7.011 1.00 78.54 ATOM 2167 O1 HOH V 214 31.582 39.863 24.269 1.00 79.14 ATOM 2168 O1 HOH V 215 −0.088 20.677 7.373 1.00 79.61 ATOM 2169 O1 HOH V 216 34.466 33.712 35.188 1.00 80.04 ATOM 2170 O1 HOH V 217 5.299 14.605 2.187 1.00 82.20 ATOM 2171 O1 HOH V 218 −0.119 43.183 −1.190 1.00 82.43 ATOM 2172 O1 HOH V 219 21.612 10.359 −10.786 1.00 83.22 ATOM 2173 O1 HOH V 220 18.145 42.688 23.379 1.00 83.87 ATOM 2174 O1 HOH V 221 38.141 26.882 26.796 1.00 84.27 ATOM 2175 O1 HOH V 222 15.645 37.869 15.459 1.00 86.80 ATOM 2176 O1 HOH V 223 33.347 0.052 24.088 1.00 88.51 ATOM 2177 O1 HOH V 224 26.717 9.812 6.181 1.00 89.08 ATOM 2178 O1 HOH V 225 13.496 7.603 15.584 1.00 89.47 ATOM 2179 O1 HOH V 226 0.897 31.611 9.140 1.00 89.58 ATOM 2180 O1 HOH V 227 13.018 26.525 −7.628 1.00 90.92 ATOM 2181 O1 HOH V 228 6.286 19.849 17.755 1.00 91.50 ATOM 2182 O1 HOH V 229 19.825 7.712 0.669 1.00 92.59 ATOM 2183 O1 HOH V 230 16.141 11.181 20.218 1.00 93.48 ATOM 2184 O1 HOH V 231 30.341 41.381 18.146 1.00 94.31 ATOM 2185 C1 CHO L 1 18.565 26.648 16.097 1.00 17.77 ATOM 2186 C4 CHO L 1 17.062 26.995 16.208 1.00 14.30 ATOM 2187 C7 CHO L 1 16.300 25.791 16.806 1.00 16.71 ATOM 2188 C9 CHO L 1 16.836 25.493 18.221 1.00 17.53 ATOM 2189 C12 CHO L 1 18.329 25.274 18.190 1.00 21.09 ATOM 2190 C13 CHO L 1 18.814 24.179 18.791 1.00 17.61 ATOM 2191 C15 CHO L 1 20.283 23.851 18.848 1.00 16.99 ATOM 2192 C18 CHO L 1 21.159 25.087 18.576 1.00 18.07 ATOM 2193 C20 CHO L 1 20.643 25.806 17.292 1.00 18.92 ATOM 2194 C22 CHO L 1 19.182 26.326 17.485 1.00 20.91 ATOM 2195 C23 CHO L 1 21.613 26.937 16.851 1.00 19.33 ATOM 2196 C26 CHO L 1 23.077 26.440 16.727 1.00 23.26 ATOM 2197 C29 CHO L 1 23.552 25.816 18.063 1.00 24.98 ATOM 2198 C30 CHO L 1 22.616 24.628 18.351 1.00 19.40 ATOM 2199 C32 CHO L 1 23.316 23.866 19.486 1.00 18.81 ATOM 2200 C35 CHO L 1 24.818 24.074 19.179 1.00 18.34 ATOM 2201 C38 CHO L 1 24.905 25.059 17.980 1.00 20.78 ATOM 2202 C40 CHO L 1 23.518 26.864 19.214 1.00 25.58 ATOM 2203 C44 CHO L 1 19.179 27.650 18.304 1.00 21.74 ATOM 2204 C48 CHO L 1 26.193 25.932 18.008 1.00 18.44 ATOM 2205 C50 CHO L 1 26.277 26.915 16.822 1.00 20.10 ATOM 2206 C54 CHO L 1 27.502 25.106 18.059 1.00 18.74 ATOM 2207 C57 CHO L 1 27.623 23.980 17.005 1.00 19.99 ATOM 2208 C60 CHO L 1 29.075 23.453 17.059 1.00 22.47 ATOM 2209 C63 CHO L 1 29.308 22.160 16.245 1.00 22.68 ATOM 2210 C65 CHO L 1 30.827 21.916 16.132 1.00 21.49 ATOM 2211 C69 CHO L 1 28.658 20.944 16.934 1.00 23.08 ATOM 2212 O73 CHO L 1 14.905 26.073 16.943 1.00 22.77 END

TABLE 9 ATOM 1 N HIS A 261 −18.369 28.759 −10.025 1.00 60.80 N ATOM 2 CA HIS A 261 −17.481 28.056 −11.002 1.00 61.14 C ATOM 3 CB HIS A 261 −18.304 27.204 −11.961 1.00 61.45 C ATOM 4 CG HIS A 261 −17.529 26.743 −13.153 1.00 63.15 C ATOM 5 ND1 HIS A 261 −17.467 27.465 −14.327 1.00 65.59 N ATOM 6 CE1 HIS A 261 −16.705 26.824 −15.195 1.00 66.06 C ATOM 7 NE2 HIS A 261 −16.255 25.723 −14.620 1.00 66.44 N ATOM 8 CD2 HIS A 261 −16.754 25.650 −13.342 1.00 65.64 C ATOM 9 C HIS A 261 −16.640 29.033 −11.812 1.00 60.44 C ATOM 10 O HIS A 261 −15.409 29.012 −11.759 1.00 60.45 O ATOM 11 N HIS A 262 −17.309 29.814 −12.647 1.00 59.75 N ATOM 12 CA HIS A 262 −16.661 30.904 −13.361 1.00 59.30 C ATOM 13 CB HIS A 262 −17.695 31.652 −14.199 1.00 58.98 C ATOM 14 CG HIS A 262 −18.358 30.763 −15.209 1.00 59.57 C ATOM 15 ND1 HIS A 262 −19.391 29.908 −14.883 1.00 59.43 N ATOM 16 CE1 HIS A 262 −19.744 29.220 −15.954 1.00 60.29 C ATOM 17 NE2 HIS A 262 −18.967 29.586 −16.959 1.00 59.72 N ATOM 18 CD2 HIS A 262 −18.082 30.538 −16.516 1.00 59.13 C ATOM 19 C HIS A 262 −15.815 31.792 −12.437 1.00 59.09 C ATOM 20 O HIS A 262 −14.698 32.162 −12.810 1.00 58.61 O ATOM 21 N LEU A 263 −16.300 32.109 −11.235 1.00 58.77 N ATOM 22 CA LEU A 263 −15.449 32.829 −10.282 1.00 58.96 C ATOM 23 CB LEU A 263 −16.221 33.286 −9.044 1.00 58.85 C ATOM 24 CG LEU A 263 −16.866 34.666 −9.101 1.00 58.28 C ATOM 25 CD1 LEU A 263 −17.642 34.934 −7.824 1.00 57.90 C ATOM 26 CD2 LEU A 263 −15.841 35.758 −9.332 1.00 57.75 C ATOM 27 C LEU A 263 −14.261 31.965 −9.840 1.00 59.44 C ATOM 28 O LEU A 263 −13.154 32.463 −9.682 1.00 59.40 O ATOM 29 N GLU A 264 −14.497 30.672 −9.638 1.00 60.29 N ATOM 30 CA GLU A 264 −13.450 29.748 −9.204 1.00 60.91 C ATOM 31 CB GLU A 264 −14.038 28.349 −8.952 1.00 61.72 C ATOM 32 CG GLU A 264 −13.227 27.462 −8.006 1.00 64.54 C ATOM 33 CD GLU A 264 −13.691 25.995 −8.002 1.00 68.63 C ATOM 34 OE1 GLU A 264 −14.800 25.693 −7.476 1.00 69.87 O ATOM 35 OE2 GLU A 264 −12.934 25.135 −8.534 1.00 70.91 O ATOM 36 C GLU A 264 −12.339 29.694 −10.251 1.00 60.26 C ATOM 37 O GLU A 264 −11.161 29.596 −9.920 1.00 60.38 O ATOM 38 N VAL A 265 −12.709 29.797 −11.516 1.00 59.34 N ATOM 39 CA VAL A 265 −11.722 29.766 −12.574 1.00 58.79 C ATOM 40 CB VAL A 265 −12.393 29.559 −13.923 1.00 58.56 C ATOM 41 CG1 VAL A 265 −11.436 29.892 −15.064 1.00 58.68 C ATOM 42 CG2 VAL A 265 −12.905 28.140 −14.025 1.00 57.58 C ATOM 43 C VAL A 265 −10.878 31.034 −12.599 1.00 58.95 C ATOM 44 O VAL A 265 −9.689 30.984 −12.896 1.00 58.69 O ATOM 45 N LEU A 266 −11.488 32.164 −12.282 1.00 59.10 N ATOM 46 CA LEU A 266 −10.780 33.433 −12.254 1.00 59.95 C ATOM 47 CB LEU A 266 −11.780 34.586 −12.145 1.00 59.85 C ATOM 48 CG LEU A 266 −12.590 34.829 −13.408 1.00 59.43 C ATOM 49 CD1 LEU A 266 −13.498 36.026 −13.226 1.00 58.82 C ATOM 50 CD2 LEU A 266 −11.655 35.012 −14.604 1.00 58.96 C ATOM 51 C LEU A 266 −9.777 33.556 −11.108 1.00 60.75 C ATOM 52 O LEU A 266 −8.907 34.423 −11.140 1.00 60.71 O ATOM 53 N PHE A 267 −9.914 32.713 −10.094 1.00 62.00 N ATOM 54 CA PHE A 267 −9.035 32.758 −8.931 1.00 63.40 C ATOM 55 CB PHE A 267 −9.881 32.790 −7.656 1.00 63.54 C ATOM 56 CG PHE A 267 −10.498 34.119 −7.397 1.00 64.83 C ATOM 57 CD1 PHE A 267 −11.812 34.368 −7.719 1.00 66.41 C ATOM 58 CE1 PHE A 267 −12.367 35.615 −7.500 1.00 67.05 C ATOM 59 CZ PHE A 267 −11.605 36.617 −6.969 1.00 67.09 C ATOM 60 CE2 PHE A 267 −10.298 36.382 −6.649 1.00 67.35 C ATOM 61 CD2 PHE A 267 −9.745 35.138 −6.864 1.00 66.42 C ATOM 62 C PHE A 267 −8.042 31.595 −8.858 1.00 64.32 C ATOM 63 O PHE A 267 −7.031 31.680 −8.158 1.00 65.16 O ATOM 64 N GLN A 268 −8.325 30.519 −9.587 1.00 64.99 N ATOM 65 CA GLN A 268 −7.514 29.299 −9.542 1.00 65.36 C ATOM 66 CB GLN A 268 −7.800 28.433 −10.770 1.00 65.80 C ATOM 67 CG GLN A 268 −7.456 26.956 −10.580 1.00 67.88 C ATOM 68 CD GLN A 268 −7.793 26.122 −11.809 1.00 70.56 C ATOM 69 OE1 GLN A 268 −8.555 26.568 −12.681 1.00 72.72 O ATOM 70 NE2 GLN A 268 −7.223 24.919 −11.891 1.00 71.16 N ATOM 71 C GLN A 268 −6.001 29.518 −9.415 1.00 64.81 C ATOM 72 O GLN A 268 −5.350 28.832 −8.630 1.00 64.77 O ATOM 73 N GLY A 269 −5.441 30.451 −10.180 1.00 64.05 N ATOM 74 CA GLY A 269 −4.005 30.686 −10.129 1.00 63.44 C ATOM 75 C GLY A 269 −3.523 31.020 −8.723 1.00 62.74 C ATOM 76 O GLY A 269 −3.081 30.147 −7.971 1.00 62.53 O ATOM 77 N PRO A 270 −3.623 32.295 −8.369 1.00 61.62 N ATOM 78 CA PRO A 270 −3.226 32.784 −7.046 1.00 60.71 C ATOM 79 CB PRO A 270 −3.788 34.203 −7.019 1.00 61.06 C ATOM 80 CG PRO A 270 −3.818 34.625 −8.460 1.00 61.54 C ATOM 81 CD PRO A 270 −4.122 33.374 −9.238 1.00 61.80 C ATOM 82 C PRO A 270 −3.805 31.980 −5.894 1.00 59.59 C ATOM 83 O PRO A 270 −3.131 31.832 −4.878 1.00 59.46 O ATOM 84 N ALA A 271 −5.019 31.464 −6.034 1.00 57.85 N ATOM 85 CA ALA A 271 −5.583 30.679 −4.955 1.00 56.85 C ATOM 86 CB ALA A 271 −6.933 30.115 −5.330 1.00 56.89 C ATOM 87 C ALA A 271 −4.642 29.553 −4.624 1.00 55.87 C ATOM 88 O ALA A 271 −4.414 29.277 −3.461 1.00 54.85 O ATOM 89 N GLU A 272 −4.123 28.906 −5.669 1.00 55.03 N ATOM 90 CA GLU A 272 −3.219 27.766 −5.542 1.00 54.75 C ATOM 91 CB GLU A 272 −2.898 27.199 −6.926 1.00 55.29 C ATOM 92 CG GLU A 272 −2.191 25.854 −6.930 1.00 58.02 C ATOM 93 CD GLU A 272 −3.117 24.691 −6.580 1.00 62.00 C ATOM 94 OE1 GLU A 272 −4.000 24.868 −5.694 1.00 62.47 O ATOM 95 OE2 GLU A 272 −2.966 23.598 −7.202 1.00 63.34 O ATOM 96 C GLU A 272 −1.923 28.139 −4.819 1.00 53.60 C ATOM 97 O GLU A 272 −1.420 27.370 −4.019 1.00 52.90 O ATOM 98 N LEU A 273 −1.392 29.323 −5.100 1.00 53.00 N ATOM 99 CA LEU A 273 −0.187 29.775 −4.440 1.00 52.74 C ATOM 100 CB LEU A 273 0.295 31.091 −5.029 1.00 53.24 C ATOM 101 CG LEU A 273 0.578 31.167 −6.522 1.00 54.92 C ATOM 102 CD1 LEU A 273 1.291 32.486 −6.819 1.00 55.95 C ATOM 103 CD2 LEU A 273 1.400 29.983 −7.007 1.00 56.45 C ATOM 104 C LEU A 273 −0.489 30.012 −2.984 1.00 51.81 C ATOM 105 O LEU A 273 0.302 29.668 −2.103 1.00 51.57 O ATOM 106 N GLU A 274 −1.638 30.629 −2.729 1.00 50.55 N ATOM 107 CA GLU A 274 −2.025 30.937 −1.362 1.00 49.74 C ATOM 108 CB GLU A 274 −3.276 31.827 −1.321 1.00 49.87 C ATOM 109 CG GLU A 274 −3.526 32.505 0.016 1.00 50.96 C ATOM 110 CD GLU A 274 −2.357 33.359 0.481 1.00 52.00 C ATOM 111 OE1 GLU A 274 −1.827 34.142 −0.341 1.00 52.15 O ATOM 112 OE2 GLU A 274 −1.974 33.236 1.665 1.00 56.29 O ATOM 113 C GLU A 274 −2.248 29.627 −0.629 1.00 48.42 C ATOM 114 O GLU A 274 −1.817 29.475 0.505 1.00 48.21 O ATOM 115 N HIS A 275 −2.879 28.668 −1.285 1.00 47.05 N ATOM 116 CA HIS A 275 −3.148 27.394 −0.623 1.00 46.52 C ATOM 117 CB HIS A 275 −3.928 26.445 −1.530 1.00 46.60 C ATOM 118 CG HIS A 275 −4.241 25.113 −0.905 1.00 48.13 C ATOM 119 ND1 HIS A 275 −5.321 24.914 −0.070 1.00 49.08 N ATOM 120 CE1 HIS A 275 −5.360 23.647 0.312 1.00 51.04 C ATOM 121 NE2 HIS A 275 −4.345 23.009 −0.248 1.00 50.51 N ATOM 122 CD2 HIS A 275 −3.631 23.903 −1.019 1.00 50.94 C ATOM 123 C HIS A 275 −1.857 26.721 −0.193 1.00 45.34 C ATOM 124 O HIS A 275 −1.766 26.218 0.917 1.00 45.39 O ATOM 125 N LEU A 276 −0.866 26.692 −1.078 1.00 44.20 N ATOM 126 CA LEU A 276 0.405 26.056 −0.762 1.00 43.43 C ATOM 127 CB LEU A 276 1.243 25.889 −2.034 1.00 43.73 C ATOM 128 CG LEU A 276 2.652 25.291 −1.877 1.00 43.56 C ATOM 129 CD1 LEU A 276 2.568 23.818 −1.557 1.00 43.50 C ATOM 130 CD2 LEU A 276 3.486 25.536 −3.127 1.00 43.26 C ATOM 131 C LEU A 276 1.172 26.881 0.310 1.00 42.47 C ATOM 132 O LEU A 276 1.879 26.346 1.153 1.00 40.97 O ATOM 133 N ALA A 277 1.035 28.190 0.302 1.00 41.76 N ATOM 134 CA ALA A 277 1.737 28.961 1.324 1.00 41.55 C ATOM 135 CB ALA A 277 1.716 30.419 1.004 1.00 41.80 C ATOM 136 C ALA A 277 1.124 28.718 2.699 1.00 41.51 C ATOM 137 O ALA A 277 1.832 28.631 3.708 1.00 41.21 O ATOM 138 N GLN A 278 −0.192 28.545 2.734 1.00 41.43 N ATOM 139 CA GLN A 278 −0.870 28.331 4.000 1.00 41.87 C ATOM 140 CB GLN A 278 −2.373 28.610 3.879 1.00 42.96 C ATOM 141 CG GLN A 278 −2.684 30.122 3.749 1.00 45.63 C ATOM 142 CD GLN A 278 −4.182 30.476 3.501 1.00 49.42 C ATOM 143 OE1 GLN A 278 −5.098 29.751 3.921 1.00 52.18 O ATOM 144 NE2 GLN A 278 −4.410 31.605 2.836 1.00 50.77 N ATOM 145 C GLN A 278 −0.570 26.945 4.521 1.00 40.99 C ATOM 146 O GLN A 278 −0.411 26.736 5.719 1.00 40.26 O ATOM 147 N ASN A 279 −0.449 25.993 3.621 1.00 40.42 N ATOM 148 CA ASN A 279 −0.117 24.635 4.021 1.00 40.51 C ATOM 149 CB ASN A 279 −0.075 23.755 2.795 1.00 41.05 C ATOM 150 CG ASN A 279 0.276 22.322 3.120 1.00 44.76 C ATOM 151 OD1 ASN A 279 −0.554 21.573 3.640 1.00 48.82 O ATOM 152 ND2 ASN A 279 1.522 21.922 2.818 1.00 51.37 N ATOM 153 C ASN A 279 1.242 24.550 4.702 1.00 39.60 C ATOM 154 O ASN A 279 1.411 23.920 5.746 1.00 40.22 O ATOM 155 N ILE A 280 2.219 25.170 4.073 1.00 38.39 N ATOM 156 CA ILE A 280 3.563 25.150 4.550 1.00 37.67 C ATOM 157 CB ILE A 280 4.493 25.612 3.419 1.00 37.61 C ATOM 158 CG1 ILE A 280 4.506 24.532 2.322 1.00 38.20 C ATOM 159 CD1 ILE A 280 5.666 24.586 1.341 1.00 39.82 C ATOM 160 CG2 ILE A 280 5.892 25.864 3.974 1.00 38.20 C ATOM 161 C ILE A 280 3.697 25.986 5.823 1.00 36.72 C ATOM 162 O ILE A 280 4.355 25.583 6.765 1.00 35.34 O ATOM 163 N SER A 281 3.060 27.146 5.842 1.00 36.72 N ATOM 164 CA SER A 281 3.018 27.979 7.043 1.00 36.93 C ATOM 165 CB SER A 281 2.091 29.161 6.831 1.00 37.23 C ATOM 166 OG SER A 281 2.681 30.069 5.909 1.00 38.94 O ATOM 167 C SER A 281 2.543 27.219 8.237 1.00 36.20 C ATOM 168 O SER A 281 3.131 27.298 9.295 1.00 35.96 O ATOM 169 N LYS A 282 1.467 26.470 8.068 1.00 36.67 N ATOM 170 CA LYS A 282 0.880 25.704 9.158 1.00 37.15 C ATOM 171 CB LYS A 282 −0.479 25.107 8.730 1.00 38.10 C ATOM 172 CG LYS A 282 −1.305 24.498 9.860 1.00 40.15 C ATOM 173 CD LYS A 282 −2.704 24.142 9.337 1.00 46.19 C ATOM 174 CE LYS A 282 −3.414 23.021 10.139 1.00 49.27 C ATOM 175 NZ LYS A 282 −3.455 21.732 9.376 1.00 51.98 N ATOM 176 C LYS A 282 1.794 24.585 9.604 1.00 36.50 C ATOM 177 O LYS A 282 1.940 24.307 10.798 1.00 35.79 O ATOM 178 N SER A 283 2.409 23.916 8.643 1.00 35.63 N ATOM 179 CA SER A 283 3.316 22.836 8.997 1.00 34.48 C ATOM 180 CB SER A 283 3.848 22.181 7.744 1.00 34.45 C ATOM 181 OG SER A 283 2.754 21.707 7.003 1.00 34.06 O ATOM 182 C SER A 283 4.441 23.381 9.830 1.00 33.76 C ATOM 183 O SER A 283 4.830 22.758 10.789 1.00 33.46 O ATOM 184 N HIS A 284 4.943 24.552 9.471 1.00 33.35 N ATOM 185 CA HIS A 284 6.007 25.195 10.224 1.00 34.42 C ATOM 186 CB HIS A 284 6.402 26.460 9.513 1.00 34.00 C ATOM 187 CG HIS A 284 7.306 27.355 10.288 1.00 34.20 C ATOM 188 ND1 HIS A 284 8.677 27.240 10.249 1.00 32.90 N ATOM 189 CE1 HIS A 284 9.221 28.201 10.968 1.00 33.90 C ATOM 190 NE2 HIS A 284 8.249 28.946 11.472 1.00 35.01 N ATOM 191 CD2 HIS A 284 7.042 28.448 11.045 1.00 36.29 C ATOM 192 C HIS A 284 5.629 25.530 11.660 1.00 35.30 C ATOM 193 O HIS A 284 6.391 25.244 12.589 1.00 34.75 O ATOM 194 N LEU A 285 4.469 26.172 11.824 1.00 36.71 N ATOM 195 CA LEU A 285 3.947 26.548 13.136 1.00 37.40 C ATOM 196 CB LEU A 285 2.579 27.208 12.997 1.00 38.70 C ATOM 197 CG LEU A 285 1.838 27.637 14.272 1.00 41.84 C ATOM 198 CD1 LEU A 285 2.525 28.826 14.913 1.00 42.97 C ATOM 199 CD2 LEU A 285 0.385 27.982 13.934 1.00 43.37 C ATOM 200 C LEU A 285 3.846 25.351 14.046 1.00 37.27 C ATOM 201 O LEU A 285 4.279 25.403 15.206 1.00 37.97 O ATOM 202 N GLU A 286 3.369 24.237 13.510 1.00 36.60 N ATOM 203 CA GLU A 286 3.134 23.058 14.337 1.00 36.96 C ATOM 204 CB GLU A 286 1.988 22.229 13.722 1.00 37.46 C ATOM 205 CG GLU A 286 0.751 23.091 13.462 1.00 42.20 C ATOM 206 CD GLU A 286 −0.487 22.289 13.142 1.00 48.25 C ATOM 207 OE1 GLU A 286 −0.343 21.219 12.510 1.00 52.12 O ATOM 208 OE2 GLU A 286 −1.601 22.726 13.534 1.00 52.12 O ATOM 209 C GLU A 286 4.350 22.157 14.572 1.00 35.80 C ATOM 210 O GLU A 286 4.231 21.190 15.303 1.00 34.55 O ATOM 211 N THR A 287 5.485 22.439 13.931 1.00 34.46 N ATOM 212 CA THR A 287 6.684 21.616 14.118 1.00 34.18 C ATOM 213 CB THR A 287 7.154 20.957 12.814 1.00 33.50 C ATOM 214 OG1 THR A 287 7.367 21.952 11.807 1.00 30.59 O ATOM 215 CG2 THR A 287 6.122 20.050 12.250 1.00 34.40 C ATOM 216 C THR A 287 7.879 22.382 14.670 1.00 34.80 C ATOM 217 O THR A 287 8.965 21.849 14.681 1.00 35.10 O ATOM 218 N CYS A 288 7.709 23.638 15.047 1.00 35.78 N ATOM 219 CA CYS A 288 8.764 24.346 15.740 1.00 36.72 C ATOM 220 CB CYS A 288 8.642 25.851 15.552 1.00 36.32 C ATOM 221 SG CYS A 288 9.235 26.481 13.966 1.00 39.84 S ATOM 222 C CYS A 288 8.682 23.996 17.230 1.00 36.71 C ATOM 223 O CYS A 288 7.602 23.895 17.792 1.00 36.87 O ATOM 224 N GLN A 289 9.830 23.812 17.866 1.00 37.19 N ATOM 225 CA GLN A 289 9.862 23.516 19.278 1.00 37.25 C ATOM 226 CB GLN A 289 11.279 23.153 19.694 1.00 37.24 C ATOM 227 CG GLN A 289 11.409 22.864 21.168 1.00 38.95 C ATOM 228 CD GLN A 289 12.661 22.072 21.551 1.00 40.39 C ATOM 229 OE1 GLN A 289 13.694 22.091 20.847 1.00 39.04 O ATOM 230 NE2 GLN A 289 12.567 21.369 22.682 1.00 38.81 N ATOM 231 C GLN A 289 9.288 24.683 20.141 1.00 37.72 C ATOM 232 O GLN A 289 8.603 24.432 21.124 1.00 37.80 O ATOM 233 N TYR A 290 9.519 25.935 19.744 1.00 38.28 N ATOM 234 CA TYR A 290 9.072 27.105 20.501 1.00 38.43 C ATOM 235 CB TYR A 290 10.268 27.813 21.152 1.00 38.66 C ATOM 236 CG TYR A 290 11.241 26.912 21.906 1.00 37.22 C ATOM 237 CD1 TYR A 290 12.438 26.540 21.332 1.00 35.94 C ATOM 238 CE1 TYR A 290 13.339 25.731 21.989 1.00 34.88 C ATOM 239 CZ TYR A 290 13.061 25.293 23.244 1.00 35.86 C ATOM 240 OH TYR A 290 13.983 24.491 23.870 1.00 34.34 O ATOM 241 CE2 TYR A 290 11.872 25.660 23.866 1.00 36.55 C ATOM 242 CD2 TYR A 290 10.978 26.487 23.193 1.00 35.75 C ATOM 243 C TYR A 290 8.329 28.158 19.650 1.00 39.65 C ATOM 244 O TYR A 290 8.582 28.309 18.443 1.00 39.27 O ATOM 245 N LEU A 291 7.443 28.924 20.296 1.00 40.18 N ATOM 246 CA LEU A 291 6.740 29.985 19.611 1.00 40.92 C ATOM 247 CB LEU A 291 5.444 30.367 20.327 1.00 41.69 C ATOM 248 CG LEU A 291 4.371 29.301 20.591 1.00 43.47 C ATOM 249 CD1 LEU A 291 3.295 29.850 21.586 1.00 45.13 C ATOM 250 CD2 LEU A 291 3.716 28.890 19.300 1.00 43.40 C ATOM 251 C LEU A 291 7.635 31.202 19.487 1.00 41.12 C ATOM 252 O LEU A 291 8.382 31.554 20.393 1.00 40.66 O ATOM 253 N ARG A 292 7.508 31.876 18.356 1.00 41.62 N ATOM 254 CA ARG A 292 8.317 33.034 18.065 1.00 42.34 C ATOM 255 CB ARG A 292 7.830 33.695 16.766 1.00 42.90 C ATOM 256 CG ARG A 292 8.712 34.814 16.241 1.00 45.07 C ATOM 257 CD ARG A 292 10.053 34.331 15.752 1.00 48.94 C ATOM 258 NE ARG A 292 10.873 35.373 15.134 1.00 50.47 N ATOM 259 CZ ARG A 292 10.786 35.746 13.871 1.00 54.17 C ATOM 260 NH1 ARG A 292 9.874 35.206 13.051 1.00 55.75 N ATOM 261 NH2 ARG A 292 11.605 36.684 13.420 1.00 55.53 N ATOM 262 C ARG A 292 8.206 34.005 19.199 1.00 42.41 C ATOM 263 O ARG A 292 9.213 34.496 19.732 1.00 41.10 O ATOM 264 N GLU A 293 6.958 34.287 19.564 1.00 43.20 N ATOM 265 CA GLU A 293 6.675 35.284 20.586 1.00 43.83 C ATOM 266 CB GLU A 293 5.164 35.519 20.679 1.00 44.63 C ATOM 267 CG GLU A 293 4.562 36.144 19.410 1.00 47.94 C ATOM 268 CD GLU A 293 4.517 35.201 18.194 1.00 51.44 C ATOM 269 OE1 GLU A 293 4.477 33.955 18.392 1.00 52.38 O ATOM 270 OE2 GLU A 293 4.516 35.711 17.033 1.00 52.22 O ATOM 271 C GLU A 293 7.299 34.887 21.928 1.00 43.00 C ATOM 272 O GLU A 293 7.878 35.732 22.598 1.00 43.39 O ATOM 273 N GLU A 294 7.207 33.613 22.303 1.00 42.66 N ATOM 274 CA GLU A 294 7.870 33.111 23.522 1.00 42.27 C ATOM 275 CB GLU A 294 7.845 31.564 23.632 1.00 43.09 C ATOM 276 CG GLU A 294 6.544 30.813 23.909 1.00 45.45 C ATOM 277 CD GLU A 294 6.529 29.398 23.262 1.00 47.89 C ATOM 278 OE1 GLU A 294 7.355 28.479 23.591 1.00 42.98 O ATOM 279 OE2 GLU A 294 5.666 29.204 22.369 1.00 50.76 O ATOM 280 C GLU A 294 9.364 33.469 23.488 1.00 40.96 C ATOM 281 O GLU A 294 9.919 33.993 24.447 1.00 40.53 O ATOM 282 N LEU A 295 10.017 33.106 22.388 1.00 39.12 N ATOM 283 CA LEU A 295 11.462 33.297 22.239 1.00 38.55 C ATOM 284 CB LEU A 295 11.959 32.681 20.918 1.00 38.19 C ATOM 285 CG LEU A 295 11.815 31.163 20.806 1.00 38.68 C ATOM 286 CD1 LEU A 295 11.654 30.733 19.372 1.00 40.29 C ATOM 287 CD2 LEU A 295 13.003 30.450 21.445 1.00 38.56 C ATOM 288 C LEU A 295 11.866 34.759 22.318 1.00 37.73 C ATOM 289 O LEU A 295 12.884 35.075 22.907 1.00 36.93 O ATOM 290 N GLN A 296 11.052 35.640 21.749 1.00 38.09 N ATOM 291 CA GLN A 296 11.323 37.083 21.755 1.00 39.08 C ATOM 292 CB GLN A 296 10.390 37.802 20.775 1.00 39.49 C ATOM 293 CG GLN A 296 10.709 37.498 19.284 1.00 43.93 C ATOM 294 CD GLN A 296 9.671 38.037 18.263 1.00 47.60 C ATOM 295 OE1 GLN A 296 8.471 38.104 18.537 1.00 50.71 O ATOM 296 NE2 GLN A 296 10.152 38.397 17.079 1.00 49.60 N ATOM 297 C GLN A 296 11.203 37.728 23.148 1.00 38.56 C ATOM 298 O GLN A 296 11.898 38.696 23.461 1.00 38.91 O ATOM 299 N GLN A 297 10.351 37.176 23.988 1.00 38.53 N ATOM 300 CA GLN A 297 10.104 37.771 25.297 1.00 38.64 C ATOM 301 CB GLN A 297 8.692 37.402 25.783 1.00 38.82 C ATOM 302 CG GLN A 297 7.621 38.365 25.195 1.00 42.59 C ATOM 303 CD GLN A 297 6.170 37.850 25.288 1.00 48.07 C ATOM 304 OE1 GLN A 297 5.797 37.151 26.239 1.00 50.31 O ATOM 305 NE2 GLN A 297 5.356 38.199 24.289 1.00 51.73 N ATOM 306 C GLN A 297 11.177 37.428 26.347 1.00 37.73 C ATOM 307 O GLN A 297 11.210 38.040 27.413 1.00 37.76 O ATOM 308 N ILE A 298 12.045 36.452 26.059 1.00 36.25 N ATOM 309 CA ILE A 298 13.087 36.084 27.007 1.00 34.28 C ATOM 310 CB ILE A 298 12.920 34.651 27.472 1.00 34.23 C ATOM 311 CG1 ILE A 298 12.999 33.705 26.282 1.00 34.17 C ATOM 312 CD1 ILE A 298 13.013 32.277 26.693 1.00 37.43 C ATOM 313 CG2 ILE A 298 11.588 34.413 28.205 1.00 36.82 C ATOM 314 C ILE A 298 14.520 36.278 26.479 1.00 32.82 C ATOM 315 O ILE A 298 15.421 35.612 26.959 1.00 32.45 O ATOM 316 N THR A 299 14.748 37.175 25.518 1.00 32.29 N ATOM 317 CA THR A 299 16.110 37.434 25.027 1.00 32.00 C ATOM 318 CB THR A 299 16.149 38.398 23.832 1.00 32.50 C ATOM 319 OG1 THR A 299 15.244 39.478 24.047 1.00 34.44 O ATOM 320 CG2 THR A 299 15.653 37.762 22.528 1.00 33.01 C ATOM 321 C THR A 299 17.000 38.007 26.104 1.00 31.05 C ATOM 322 O THR A 299 18.212 37.917 26.015 1.00 30.68 O ATOM 323 N TRP A 300 16.412 38.607 27.132 1.00 30.79 N ATOM 324 CA TRP A 300 17.218 39.162 28.237 1.00 29.80 C ATOM 325 CB TRP A 300 16.413 40.155 29.094 1.00 29.57 C ATOM 326 CG TRP A 300 15.189 39.547 29.664 1.00 27.22 C ATOM 327 CD1 TRP A 300 13.988 39.423 29.044 1.00 25.70 C ATOM 328 NE1 TRP A 300 13.096 38.775 29.862 1.00 24.08 N ATOM 329 CE2 TRP A 300 13.727 38.462 31.033 1.00 24.93 C ATOM 330 CD2 TRP A 300 15.045 38.926 30.936 1.00 23.62 C ATOM 331 CE3 TRP A 300 15.884 38.761 32.030 1.00 26.31 C ATOM 332 CZ3 TRP A 300 15.415 38.153 33.128 1.00 27.39 C ATOM 333 CH2 TRP A 300 14.083 37.700 33.201 1.00 28.78 C ATOM 334 CZ2 TRP A 300 13.231 37.857 32.168 1.00 24.74 C ATOM 335 C TRP A 300 17.803 38.099 29.155 1.00 29.45 C ATOM 336 O TRP A 300 18.751 38.365 29.906 1.00 30.38 O ATOM 337 N GLN A 301 17.231 36.897 29.103 1.00 29.27 N ATOM 338 CA GLN A 301 17.695 35.781 29.923 1.00 29.27 C ATOM 339 CB GLN A 301 16.616 34.701 30.038 1.00 28.84 C ATOM 340 CG GLN A 301 15.419 35.171 30.791 1.00 30.22 C ATOM 341 CD GLN A 301 14.251 34.170 30.897 1.00 33.05 C ATOM 342 OE1 GLN A 301 14.340 33.032 30.464 1.00 32.79 O ATOM 343 NE2 GLN A 301 13.144 34.633 31.479 1.00 34.45 N ATOM 344 C GLN A 301 18.964 35.186 29.327 1.00 29.50 C ATOM 345 O GLN A 301 18.926 34.117 28.725 1.00 30.22 O ATOM 346 N THR A 302 20.081 35.884 29.484 1.00 29.33 N ATOM 347 CA THR A 302 21.372 35.407 29.007 1.00 29.03 C ATOM 348 CB THR A 302 22.271 36.588 28.567 1.00 29.13 C ATOM 349 OG1 THR A 302 22.307 37.572 29.603 1.00 28.27 O ATOM 350 CG2 THR A 302 21.695 37.317 27.362 1.00 29.18 C ATOM 351 C THR A 302 22.024 34.662 30.165 1.00 29.23 C ATOM 352 O THR A 302 21.615 34.836 31.308 1.00 29.31 O ATOM 353 N PHE A 303 22.987 33.791 29.874 1.00 29.05 N ATOM 354 CA PHE A 303 23.704 33.101 30.929 1.00 29.57 C ATOM 355 CB PHE A 303 24.678 32.033 30.380 1.00 29.12 C ATOM 356 CG PHE A 303 23.998 30.815 29.837 1.00 27.07 C ATOM 357 CD1 PHE A 303 23.798 30.691 28.475 1.00 27.05 C ATOM 358 CE1 PHE A 303 23.156 29.630 27.957 1.00 27.11 C ATOM 359 CZ PHE A 303 22.699 28.639 28.795 1.00 27.76 C ATOM 360 CE2 PHE A 303 22.884 28.746 30.156 1.00 27.13 C ATOM 361 CD2 PHE A 303 23.530 29.833 30.669 1.00 26.38 C ATOM 362 C PHE A 303 24.461 34.134 31.780 1.00 30.22 C ATOM 363 O PHE A 303 24.913 35.153 31.291 1.00 30.40 O ATOM 364 N LEU A 304 24.598 33.854 33.053 1.00 31.25 N ATOM 365 CA LEU A 304 25.332 34.733 33.954 1.00 32.65 C ATOM 366 CB LEU A 304 24.930 34.475 35.390 1.00 32.80 C ATOM 367 CG LEU A 304 23.457 34.647 35.722 1.00 33.60 C ATOM 368 CD1 LEU A 304 23.213 34.101 37.076 1.00 35.11 C ATOM 369 CD2 LEU A 304 23.051 36.084 35.695 1.00 35.33 C ATOM 370 C LEU A 304 26.800 34.424 33.797 1.00 34.30 C ATOM 371 O LEU A 304 27.171 33.345 33.332 1.00 32.86 O ATOM 372 N GLN A 305 27.647 35.360 34.195 1.00 36.15 N ATOM 373 CA GLN A 305 29.077 35.180 34.006 1.00 38.54 C ATOM 374 CB GLN A 305 29.852 36.381 34.584 1.00 39.68 C ATOM 375 CG GLN A 305 31.293 36.596 34.029 1.00 42.48 C ATOM 376 CD GLN A 305 31.436 36.533 32.488 1.00 46.39 C ATOM 377 OE1 GLN A 305 30.636 37.118 31.720 1.00 46.08 O ATOM 378 NE2 GLN A 305 32.497 35.850 32.041 1.00 48.27 N ATOM 379 C GLN A 305 29.584 33.832 34.575 1.00 38.86 C ATOM 380 O GLN A 305 30.428 33.194 33.968 1.00 39.34 O ATOM 381 N GLU A 306 29.031 33.391 35.698 1.00 39.71 N ATOM 382 CA GLU A 306 29.451 32.155 36.350 1.00 39.99 C ATOM 383 CB GLU A 306 28.756 31.992 37.705 1.00 41.15 C ATOM 384 CG GLU A 306 29.089 33.078 38.735 1.00 47.39 C ATOM 385 CD GLU A 306 28.167 33.080 39.980 1.00 55.43 C ATOM 386 OE1 GLU A 306 27.643 31.999 40.357 1.00 59.46 O ATOM 387 OE2 GLU A 306 27.962 34.167 40.612 1.00 60.68 O ATOM 388 C GLU A 306 29.132 30.952 35.472 1.00 38.37 C ATOM 389 O GLU A 306 29.926 30.022 35.353 1.00 38.01 O ATOM 390 N GLU A 307 27.943 30.967 34.889 1.00 36.34 N ATOM 391 CA GLU A 307 27.514 29.927 33.988 1.00 34.63 C ATOM 392 CB GLU A 307 26.032 30.117 33.642 1.00 35.14 C ATOM 393 CG GLU A 307 25.062 30.047 34.823 1.00 34.93 C ATOM 394 CD GLU A 307 23.620 30.319 34.412 1.00 36.18 C ATOM 395 OE1 GLU A 307 22.785 29.382 34.543 1.00 36.82 O ATOM 396 OE2 GLU A 307 23.312 31.467 33.946 1.00 32.29 O ATOM 397 C GLU A 307 28.395 29.957 32.716 1.00 33.42 C ATOM 398 O GLU A 307 28.752 28.907 32.177 1.00 30.28 O ATOM 399 N ILE A 308 28.778 31.149 32.264 1.00 32.73 N ATOM 400 CA ILE A 308 29.593 31.251 31.062 1.00 33.52 C ATOM 401 CB ILE A 308 29.723 32.701 30.595 1.00 33.62 C ATOM 402 CG1 ILE A 308 28.384 33.198 30.061 1.00 34.47 C ATOM 403 CD1 ILE A 308 28.385 34.618 29.697 1.00 34.55 C ATOM 404 CG2 ILE A 308 30.758 32.864 29.484 1.00 33.46 C ATOM 405 C ILE A 308 30.933 30.564 31.324 1.00 34.15 C ATOM 406 O ILE A 308 31.373 29.709 30.560 1.00 33.82 O ATOM 407 N GLU A 309 31.549 30.899 32.447 1.00 35.66 N ATOM 408 CA GLU A 309 32.813 30.284 32.858 1.00 36.34 C ATOM 409 CB GLU A 309 33.280 30.879 34.199 1.00 37.37 C ATOM 410 CG GLU A 309 33.860 32.290 34.048 1.00 41.64 C ATOM 411 CD GLU A 309 33.687 33.171 35.295 1.00 46.42 C ATOM 412 OE1 GLU A 309 33.419 32.615 36.387 1.00 49.14 O ATOM 413 OE2 GLU A 309 33.805 34.426 35.174 1.00 51.22 O ATOM 414 C GLU A 309 32.718 28.766 32.941 1.00 35.17 C ATOM 415 O GLU A 309 33.580 28.072 32.431 1.00 35.55 O ATOM 416 N ASN A 310 31.679 28.249 33.578 1.00 34.21 N ATOM 417 CA ASN A 310 31.478 26.817 33.603 1.00 34.07 C ATOM 418 CB ASN A 310 30.168 26.511 34.282 1.00 35.39 C ATOM 419 CG ASN A 310 29.871 25.036 34.346 1.00 38.20 C ATOM 420 OD1 ASN A 310 30.608 24.260 34.994 1.00 45.99 O ATOM 421 ND2 ASN A 310 28.778 24.629 33.712 1.00 42.62 N ATOM 422 C ASN A 310 31.488 26.202 32.212 1.00 33.34 C ATOM 423 O ASN A 310 32.171 25.193 31.987 1.00 33.73 O ATOM 424 N TYR A 311 30.780 26.795 31.247 1.00 31.41 N ATOM 425 CA TYR A 311 30.793 26.215 29.919 1.00 30.92 C ATOM 426 CB TYR A 311 29.821 26.904 28.959 1.00 30.60 C ATOM 427 CG TYR A 311 28.362 26.519 29.117 1.00 29.73 C ATOM 428 CD1 TYR A 311 27.421 27.465 29.445 1.00 28.73 C ATOM 429 CE1 TYR A 311 26.090 27.149 29.590 1.00 29.50 C ATOM 430 CZ TYR A 311 25.671 25.875 29.403 1.00 29.74 C ATOM 431 OH TYR A 311 24.332 25.610 29.557 1.00 32.23 O ATOM 432 CE2 TYR A 311 26.578 24.897 29.056 1.00 29.37 C ATOM 433 CD2 TYR A 311 27.925 25.224 28.915 1.00 29.13 C ATOM 434 C TYR A 311 32.192 26.310 29.367 1.00 31.46 C ATOM 435 O TYR A 311 32.635 25.434 28.636 1.00 30.86 O ATOM 436 N GLN A 312 32.890 27.398 29.688 1.00 32.56 N ATOM 437 CA GLN A 312 34.251 27.554 29.209 1.00 33.54 C ATOM 438 CB GLN A 312 34.706 29.010 29.300 1.00 33.50 C ATOM 439 CG GLN A 312 34.082 29.859 28.239 1.00 33.49 C ATOM 440 CD GLN A 312 34.392 31.302 28.461 1.00 34.18 C ATOM 441 OE1 GLN A 312 34.841 31.667 29.542 1.00 35.47 O ATOM 442 NE2 GLN A 312 34.172 32.127 27.449 1.00 31.68 N ATOM 443 C GLN A 312 35.202 26.603 29.928 1.00 34.41 C ATOM 444 O GLN A 312 36.250 26.270 29.394 1.00 34.43 O ATOM 445 N ASN A 313 34.834 26.151 31.116 1.00 35.17 N ATOM 446 CA ASN A 313 35.680 25.192 31.827 1.00 36.70 C ATOM 447 CB ASN A 313 35.383 25.209 33.333 1.00 37.66 C ATOM 448 CG ASN A 313 35.992 26.423 34.051 1.00 41.22 C ATOM 449 OD1 ASN A 313 36.882 27.096 33.522 1.00 42.54 O ATOM 450 ND2 ASN A 313 35.478 26.717 35.265 1.00 44.69 N ATOM 451 C ASN A 313 35.531 23.745 31.310 1.00 36.84 C ATOM 452 O ASN A 313 36.405 22.889 31.568 1.00 36.22 O ATOM 453 N LYS A 314 34.412 23.459 30.619 1.00 36.29 N ATOM 454 CA LYS A 314 34.166 22.111 30.110 1.00 35.35 C ATOM 455 CB LYS A 314 32.761 21.940 29.527 1.00 35.14 C ATOM 456 CG LYS A 314 31.628 22.032 30.526 1.00 35.45 C ATOM 457 CD LYS A 314 30.290 21.978 29.787 1.00 38.14 C ATOM 458 CE LYS A 314 29.085 22.009 30.733 1.00 39.70 C ATOM 459 NZ LYS A 314 29.206 21.049 31.917 1.00 44.38 N ATOM 460 C LYS A 314 35.186 21.752 29.052 1.00 35.29 C ATOM 461 O LYS A 314 35.676 22.605 28.307 1.00 35.12 O ATOM 462 N GLN A 315 35.484 20.452 29.000 1.00 34.85 N ATOM 463 CA GLN A 315 36.430 19.906 28.048 1.00 34.64 C ATOM 464 CB GLN A 315 36.771 18.469 28.417 1.00 34.90 C ATOM 465 CG GLN A 315 37.502 18.260 29.733 1.00 39.29 C ATOM 466 CD GLN A 315 38.919 18.804 29.697 1.00 44.94 C ATOM 467 OE1 GLN A 315 39.685 18.490 28.787 1.00 50.63 O ATOM 468 NE2 GLN A 315 39.264 19.634 30.677 1.00 47.61 N ATOM 469 C GLN A 315 35.846 19.884 26.647 1.00 33.86 C ATOM 470 O GLN A 315 34.631 19.748 26.460 1.00 32.99 O ATOM 471 N ARG A 316 36.729 19.965 25.664 1.00 32.95 N ATOM 472 CA ARG A 316 36.315 19.977 24.292 1.00 32.86 C ATOM 473 CB ARG A 316 37.519 19.829 23.385 1.00 33.76 C ATOM 474 CG ARG A 316 37.205 20.195 21.947 1.00 38.32 C ATOM 475 CD ARG A 316 38.414 20.275 21.047 1.00 43.87 C ATOM 476 NE ARG A 316 38.022 20.301 19.640 1.00 49.79 N ATOM 477 CZ ARG A 316 38.804 19.922 18.624 1.00 53.81 C ATOM 478 NH1 ARG A 316 40.036 19.479 18.847 1.00 55.22 N ATOM 479 NH2 ARG A 316 38.347 19.990 17.381 1.00 55.07 N ATOM 480 C ARG A 316 35.289 18.895 23.966 1.00 31.22 C ATOM 481 O ARG A 316 34.241 19.187 23.405 1.00 28.96 O ATOM 482 N GLU A 317 35.575 17.649 24.327 1.00 30.76 N ATOM 483 CA GLU A 317 34.680 16.574 23.930 1.00 30.63 C ATOM 484 CB GLU A 317 35.315 15.181 24.082 1.00 31.32 C ATOM 485 CG GLU A 317 35.547 14.697 25.484 1.00 33.23 C ATOM 486 CD GLU A 317 36.850 15.194 26.090 1.00 38.72 C ATOM 487 OE1 GLU A 317 37.349 14.502 27.024 1.00 44.77 O ATOM 488 OE2 GLU A 317 37.365 16.259 25.674 1.00 34.98 O ATOM 489 C GLU A 317 33.351 16.695 24.640 1.00 29.33 C ATOM 490 O GLU A 317 32.344 16.314 24.099 1.00 30.11 O ATOM 491 N VAL A 318 33.365 17.256 25.829 1.00 27.92 N ATOM 492 CA VAL A 318 32.173 17.464 26.628 1.00 27.86 C ATOM 493 CB VAL A 318 32.529 17.835 28.082 1.00 28.20 C ATOM 494 CG1 VAL A 318 31.275 18.177 28.870 1.00 28.77 C ATOM 495 CG2 VAL A 318 33.263 16.646 28.741 1.00 29.97 C ATOM 496 C VAL A 318 31.244 18.528 26.013 1.00 27.21 C ATOM 497 O VAL A 318 30.048 18.287 25.886 1.00 26.50 O ATOM 498 N MET A 319 31.799 19.670 25.603 1.00 26.29 N ATOM 499 CA MET A 319 31.018 20.716 24.961 1.00 26.24 C ATOM 500 CB MET A 319 31.852 22.004 24.831 1.00 27.30 C ATOM 501 CG MET A 319 31.050 23.268 24.597 1.00 28.90 C ATOM 502 SD MET A 319 29.794 23.654 25.828 1.00 33.36 S ATOM 503 CE MET A 319 28.848 24.807 24.932 1.00 31.15 C ATOM 504 C MET A 319 30.472 20.228 23.615 1.00 25.53 C ATOM 505 O MET A 319 29.325 20.447 23.281 1.00 25.99 O ATOM 506 N TRP A 320 31.267 19.511 22.857 1.00 25.05 N ATOM 507 CA TRP A 320 30.790 18.939 21.621 1.00 24.82 C ATOM 508 CB TRP A 320 31.923 18.183 20.921 1.00 24.80 C ATOM 509 CG TRP A 320 32.634 18.949 19.867 1.00 27.31 C ATOM 510 CD1 TRP A 320 33.705 19.786 20.039 1.00 30.43 C ATOM 511 NE1 TRP A 320 34.100 20.301 18.831 1.00 31.02 N ATOM 512 CE2 TRP A 320 33.268 19.826 17.854 1.00 28.25 C ATOM 513 CD2 TRP A 320 32.338 18.969 18.470 1.00 28.17 C ATOM 514 CE3 TRP A 320 31.357 18.366 17.675 1.00 29.23 C ATOM 515 CZ3 TRP A 320 31.356 18.606 16.320 1.00 28.97 C ATOM 516 CH2 TRP A 320 32.293 19.478 15.739 1.00 28.19 C ATOM 517 CZ2 TRP A 320 33.260 20.086 16.492 1.00 28.61 C ATOM 518 C TRP A 320 29.594 17.984 21.832 1.00 24.11 C ATOM 519 O TRP A 320 28.638 18.021 21.080 1.00 23.54 O ATOM 520 N GLN A 321 29.644 17.118 22.832 1.00 24.43 N ATOM 521 CA GLN A 321 28.544 16.178 23.043 1.00 24.39 C ATOM 522 CB GLN A 321 28.836 15.179 24.168 1.00 24.76 C ATOM 523 CG GLN A 321 27.876 14.013 24.140 1.00 24.84 C ATOM 524 CD GLN A 321 27.120 13.800 25.417 1.00 26.37 C ATOM 525 OE1 GLN A 321 27.146 14.650 26.271 1.00 29.09 O ATOM 526 NE2 GLN A 321 26.444 12.627 25.556 1.00 26.55 N ATOM 527 C GLN A 321 27.249 16.900 23.359 1.00 24.19 C ATOM 528 O GLN A 321 26.180 16.559 22.832 1.00 24.08 O ATOM 529 N LEU A 322 27.368 17.924 24.178 1.00 24.78 N ATOM 530 CA LEU A 322 26.236 18.733 24.579 1.00 25.69 C ATOM 531 CB LEU A 322 26.644 19.732 25.683 1.00 26.07 C ATOM 532 CG LEU A 322 25.622 20.738 26.235 1.00 27.41 C ATOM 533 CD1 LEU A 322 24.406 20.074 26.909 1.00 29.40 C ATOM 534 CD2 LEU A 322 26.277 21.639 27.190 1.00 30.22 C ATOM 535 C LEU A 322 25.615 19.430 23.374 1.00 26.06 C ATOM 536 O LEU A 322 24.406 19.285 23.125 1.00 26.90 O ATOM 537 N CYS A 323 26.420 20.140 22.587 1.00 25.58 N ATOM 538 CA CYS A 323 25.893 20.774 21.384 1.00 25.11 C ATOM 539 CB CYS A 323 26.996 21.554 20.686 1.00 25.72 C ATOM 540 SG CYS A 323 27.607 22.944 21.675 1.00 29.20 S ATOM 541 C CYS A 323 25.246 19.776 20.419 1.00 25.04 C ATOM 542 O CYS A 323 24.215 20.057 19.816 1.00 23.70 O ATOM 543 N ALA A 324 25.846 18.604 20.272 1.00 24.13 N ATOM 544 CA ALA A 324 25.275 17.625 19.398 1.00 23.43 C ATOM 545 CB ALA A 324 26.226 16.462 19.222 1.00 24.05 C ATOM 546 C ALA A 324 23.913 17.141 19.912 1.00 23.43 C ATOM 547 O ALA A 324 23.011 16.938 19.125 1.00 22.57 O ATOM 548 N ILE A 325 23.776 16.932 21.218 1.00 23.59 N ATOM 549 CA ILE A 325 22.482 16.591 21.791 1.00 24.38 C ATOM 550 CB ILE A 325 22.556 16.407 23.323 1.00 24.71 C ATOM 551 CG1 ILE A 325 23.293 15.136 23.709 1.00 25.02 C ATOM 552 CD1 ILE A 325 23.649 15.149 25.190 1.00 27.28 C ATOM 553 CG2 ILE A 325 21.158 16.398 23.942 1.00 22.26 C ATOM 554 C ILE A 325 21.479 17.705 21.501 1.00 24.86 C ATOM 555 O ILE A 325 20.384 17.453 21.044 1.00 24.56 O ATOM 556 N LYS A 326 21.856 18.940 21.772 1.00 25.56 N ATOM 557 CA LYS A 326 20.926 20.047 21.580 1.00 26.26 C ATOM 558 CB LYS A 326 21.489 21.318 22.184 1.00 26.21 C ATOM 559 CG LYS A 326 21.741 21.248 23.681 1.00 29.37 C ATOM 560 CD LYS A 326 20.479 20.914 24.433 1.00 33.36 C ATOM 561 CE LYS A 326 20.725 20.802 25.926 1.00 36.77 C ATOM 562 NZ LYS A 326 19.694 19.921 26.567 1.00 37.66 N ATOM 563 C LYS A 326 20.520 20.209 20.094 1.00 26.40 C ATOM 564 O LYS A 326 19.348 20.386 19.803 1.00 25.16 O ATOM 565 N ILE A 327 21.480 20.110 19.175 1.00 26.86 N ATOM 566 CA ILE A 327 21.208 20.174 17.740 1.00 28.16 C ATOM 567 CB ILE A 327 22.511 20.235 16.930 1.00 29.15 C ATOM 568 CG1 ILE A 327 22.666 21.619 16.335 1.00 35.09 C ATOM 569 CD1 ILE A 327 23.951 21.810 15.538 1.00 39.84 C ATOM 570 CG2 ILE A 327 22.465 19.314 15.745 1.00 31.87 C ATOM 571 C ILE A 327 20.378 19.015 17.250 1.00 27.66 C ATOM 572 O ILE A 327 19.544 19.152 16.361 1.00 27.77 O ATOM 573 N THR A 328 20.599 17.855 17.811 1.00 27.88 N ATOM 574 CA THR A 328 19.810 16.726 17.415 1.00 28.75 C ATOM 575 CB THR A 328 20.328 15.479 18.028 1.00 29.15 C ATOM 576 OG1 THR A 328 21.665 15.267 17.581 1.00 28.97 O ATOM 577 CG2 THR A 328 19.547 14.287 17.518 1.00 30.09 C ATOM 578 C THR A 328 18.343 16.927 17.776 1.00 28.80 C ATOM 579 O THR A 328 17.496 16.567 16.986 1.00 27.42 O ATOM 580 N GLU A 329 18.051 17.530 18.928 1.00 29.14 N ATOM 581 CA GLU A 329 16.658 17.852 19.278 1.00 30.60 C ATOM 582 CB GLU A 329 16.546 18.559 20.643 1.00 31.73 C ATOM 583 CG GLU A 329 17.198 17.863 21.820 1.00 37.45 C ATOM 584 CD GLU A 329 17.178 18.684 23.122 1.00 43.70 C ATOM 585 OE1 GLU A 329 16.578 19.802 23.159 1.00 42.77 O ATOM 586 OE2 GLU A 329 17.756 18.174 24.135 1.00 49.00 O ATOM 587 C GLU A 329 15.985 18.751 18.215 1.00 29.00 C ATOM 588 O GLU A 329 14.864 18.502 17.776 1.00 28.96 O ATOM 589 N ALA A 330 16.648 19.829 17.825 1.00 27.92 N ATOM 590 CA ALA A 330 16.105 20.694 16.793 1.00 27.01 C ATOM 591 CB ALA A 330 16.981 21.881 16.610 1.00 27.09 C ATOM 592 C ALA A 330 15.900 19.967 15.447 1.00 27.24 C ATOM 593 O ALA A 330 14.911 20.208 14.753 1.00 27.51 O ATOM 594 N ILE A 331 16.837 19.109 15.070 1.00 26.90 N ATOM 595 CA ILE A 331 16.695 18.308 13.860 1.00 27.25 C ATOM 596 CB ILE A 331 17.973 17.520 13.585 1.00 26.89 C ATOM 597 CG1 ILE A 331 19.052 18.507 13.149 1.00 27.96 C ATOM 598 CD1 ILE A 331 20.406 17.877 12.923 1.00 29.48 C ATOM 599 CG2 ILE A 331 17.766 16.414 12.484 1.00 26.39 C ATOM 600 C ILE A 331 15.470 17.390 13.885 1.00 27.69 C ATOM 601 O ILE A 331 14.810 17.205 12.859 1.00 27.06 O ATOM 602 N GLN A 332 15.160 16.830 15.041 1.00 28.59 N ATOM 603 CA GLN A 332 13.987 15.988 15.167 1.00 30.50 C ATOM 604 CB GLN A 332 13.849 15.439 16.579 1.00 31.71 C ATOM 605 CG GLN A 332 14.526 14.109 16.681 1.00 36.53 C ATOM 606 CD GLN A 332 14.827 13.693 18.084 1.00 43.18 C ATOM 607 OE1 GLN A 332 14.295 14.274 19.043 1.00 46.43 O ATOM 608 NE2 GLN A 332 15.717 12.680 18.228 1.00 46.39 N ATOM 609 C GLN A 332 12.736 16.742 14.763 1.00 30.16 C ATOM 610 O GLN A 332 11.879 16.192 14.086 1.00 29.89 O ATOM 611 N TYR A 333 12.666 18.012 15.142 1.00 29.91 N ATOM 612 CA TYR A 333 11.548 18.863 14.773 1.00 29.79 C ATOM 613 CB TYR A 333 11.552 20.152 15.632 1.00 30.02 C ATOM 614 CG TYR A 333 11.052 19.929 17.038 1.00 30.98 C ATOM 615 CD1 TYR A 333 11.928 19.789 18.095 1.00 32.18 C ATOM 616 CE1 TYR A 333 11.460 19.555 19.372 1.00 34.65 C ATOM 617 CZ TYR A 333 10.097 19.474 19.605 1.00 35.79 C ATOM 618 OH TYR A 333 9.635 19.256 20.875 1.00 40.22 O ATOM 619 CE2 TYR A 333 9.207 19.621 18.590 1.00 34.47 C ATOM 620 CD2 TYR A 333 9.687 19.858 17.305 1.00 34.75 C ATOM 621 C TYR A 333 11.543 19.187 13.272 1.00 29.21 C ATOM 622 O TYR A 333 10.498 19.330 12.658 1.00 29.48 O ATOM 623 N VAL A 334 12.711 19.337 12.683 1.00 28.49 N ATOM 624 CA VAL A 334 12.781 19.602 11.247 1.00 28.13 C ATOM 625 CB VAL A 334 14.204 20.060 10.872 1.00 28.00 C ATOM 626 CG1 VAL A 334 14.470 19.953 9.349 1.00 28.89 C ATOM 627 CG2 VAL A 334 14.441 21.427 11.401 1.00 26.70 C ATOM 628 C VAL A 334 12.347 18.349 10.439 1.00 27.92 C ATOM 629 O VAL A 334 11.770 18.465 9.378 1.00 26.84 O ATOM 630 N VAL A 335 12.612 17.158 10.948 1.00 28.87 N ATOM 631 CA VAL A 335 12.151 15.943 10.276 1.00 30.06 C ATOM 632 CB VAL A 335 12.737 14.699 10.894 1.00 30.00 C ATOM 633 CG1 VAL A 335 12.072 13.487 10.339 1.00 32.57 C ATOM 634 CG2 VAL A 335 14.210 14.592 10.597 1.00 30.15 C ATOM 635 C VAL A 335 10.588 15.881 10.266 1.00 30.90 C ATOM 636 O VAL A 335 9.984 15.468 9.263 1.00 29.27 O ATOM 637 N GLU A 336 9.953 16.356 11.344 1.00 31.20 N ATOM 638 CA GLU A 336 8.489 16.425 11.393 1.00 32.50 C ATOM 639 CB GLU A 336 7.961 16.735 12.812 1.00 33.25 C ATOM 640 CG GLU A 336 8.283 15.671 13.862 1.00 36.91 C ATOM 641 CD GLU A 336 7.627 14.299 13.616 1.00 44.18 C ATOM 642 OE1 GLU A 336 6.463 14.240 13.123 1.00 48.70 O ATOM 643 OE2 GLU A 336 8.276 13.256 13.928 1.00 47.83 O ATOM 644 C GLU A 336 7.980 17.440 10.380 1.00 31.88 C ATOM 645 O GLU A 336 6.994 17.194 9.697 1.00 32.26 O ATOM 646 N PHE A 337 8.654 18.569 10.246 1.00 31.25 N ATOM 647 CA PHE A 337 8.315 19.488 9.189 1.00 31.26 C ATOM 648 CB PHE A 337 9.270 20.670 9.251 1.00 31.46 C ATOM 649 CG PHE A 337 9.017 21.746 8.229 1.00 30.00 C ATOM 650 CD1 PHE A 337 7.842 22.467 8.237 1.00 29.18 C ATOM 651 CE1 PHE A 337 7.643 23.484 7.357 1.00 29.25 C ATOM 652 CZ PHE A 337 8.620 23.811 6.418 1.00 30.20 C ATOM 653 CE2 PHE A 337 9.799 23.094 6.381 1.00 30.76 C ATOM 654 CD2 PHE A 337 9.988 22.059 7.287 1.00 31.21 C ATOM 655 C PHE A 337 8.364 18.826 7.779 1.00 32.11 C ATOM 656 O PHE A 337 7.402 18.929 7.011 1.00 31.39 O ATOM 657 N ALA A 338 9.479 18.176 7.438 1.00 32.85 N ATOM 658 CA ALA A 338 9.618 17.536 6.134 1.00 34.45 C ATOM 659 CB ALA A 338 10.936 16.787 6.029 1.00 34.40 C ATOM 660 C ALA A 338 8.448 16.593 5.849 1.00 35.78 C ATOM 661 O ALA A 338 7.848 16.667 4.806 1.00 35.41 O ATOM 662 N LYS A 339 8.127 15.725 6.790 1.00 37.72 N ATOM 663 CA LYS A 339 7.058 14.776 6.598 1.00 39.80 C ATOM 664 CB LYS A 339 6.761 14.056 7.886 1.00 40.02 C ATOM 665 CG LYS A 339 7.901 13.158 8.291 1.00 42.45 C ATOM 666 CD LYS A 339 7.440 11.942 9.028 1.00 44.60 C ATOM 667 CE LYS A 339 7.206 12.224 10.454 1.00 46.22 C ATOM 668 NZ LYS A 339 7.415 10.966 11.174 1.00 46.80 N ATOM 669 C LYS A 339 5.777 15.391 6.072 1.00 41.25 C ATOM 670 O LYS A 339 5.091 14.789 5.275 1.00 41.74 O ATOM 671 N ARG A 340 5.485 16.605 6.497 1.00 42.74 N ATOM 672 CA ARG A 340 4.266 17.275 6.127 1.00 43.70 C ATOM 673 CB ARG A 340 3.887 18.223 7.229 1.00 43.78 C ATOM 674 CG ARG A 340 3.550 17.533 8.494 1.00 45.03 C ATOM 675 CD ARG A 340 3.273 18.483 9.594 1.00 46.53 C ATOM 676 NE ARG A 340 3.333 17.821 10.887 1.00 49.07 N ATOM 677 CZ ARG A 340 2.578 18.165 11.915 1.00 51.42 C ATOM 678 NH1 ARG A 340 1.697 19.167 11.779 1.00 53.86 N ATOM 679 NH2 ARG A 340 2.691 17.510 13.063 1.00 50.56 N ATOM 680 C ARG A 340 4.355 18.086 4.858 1.00 44.39 C ATOM 681 O ARG A 340 3.381 18.710 4.473 1.00 44.75 O ATOM 682 N ILE A 341 5.516 18.136 4.231 1.00 44.93 N ATOM 683 CA ILE A 341 5.626 18.907 3.015 1.00 45.79 C ATOM 684 CB ILE A 341 7.073 19.340 2.776 1.00 45.44 C ATOM 685 CG1 ILE A 341 7.446 20.384 3.818 1.00 45.69 C ATOM 686 CD1 ILE A 341 8.901 20.710 3.847 1.00 46.77 C ATOM 687 CG2 ILE A 341 7.240 19.881 1.357 1.00 45.67 C ATOM 688 C ILE A 341 5.080 18.035 1.895 1.00 46.85 C ATOM 689 O ILE A 341 5.483 16.883 1.738 1.00 46.56 O ATOM 690 N ASP A 342 4.148 18.593 1.129 1.00 48.25 N ATOM 691 CA ASP A 342 3.476 17.821 0.093 1.00 49.01 C ATOM 692 CB ASP A 342 2.306 18.611 −0.490 1.00 50.45 C ATOM 693 CG ASP A 342 1.152 18.788 0.493 1.00 53.95 C ATOM 694 OD1 ASP A 342 0.695 17.786 1.084 1.00 58.87 O ATOM 695 OD2 ASP A 342 0.636 19.914 0.713 1.00 59.55 O ATOM 696 C ASP A 342 4.424 17.453 −1.031 1.00 48.01 C ATOM 697 O ASP A 342 4.927 18.316 −1.747 1.00 47.92 O ATOM 698 N GLY A 343 4.642 16.155 −1.185 1.00 46.69 N ATOM 699 CA GLY A 343 5.544 15.642 −2.199 1.00 45.52 C ATOM 700 C GLY A 343 6.710 14.888 −1.596 1.00 43.87 C ATOM 701 O GLY A 343 7.268 13.970 −2.205 1.00 43.67 O ATOM 702 N PHE A 344 7.045 15.232 −0.365 1.00 41.81 N ATOM 703 CA PHE A 344 8.221 14.673 0.266 1.00 40.97 C ATOM 704 CB PHE A 344 8.588 15.453 1.533 1.00 40.64 C ATOM 705 CG PHE A 344 9.850 14.977 2.170 1.00 38.48 C ATOM 706 CD1 PHE A 344 11.081 15.500 1.814 1.00 36.83 C ATOM 707 CE1 PHE A 344 12.245 15.020 2.396 1.00 37.61 C ATOM 708 CZ PHE A 344 12.190 14.000 3.311 1.00 36.20 C ATOM 709 CE2 PHE A 344 10.961 13.456 3.658 1.00 36.79 C ATOM 710 CD2 PHE A 344 9.809 13.939 3.084 1.00 36.78 C ATOM 711 C PHE A 344 7.999 13.204 0.543 1.00 41.48 C ATOM 712 O PHE A 344 8.864 12.366 0.254 1.00 41.42 O ATOM 713 N MET A 345 6.814 12.881 1.056 1.00 42.09 N ATOM 714 CA MET A 345 6.447 11.536 1.370 1.00 43.10 C ATOM 715 CB MET A 345 5.247 11.496 2.326 1.00 43.84 C ATOM 716 CG MET A 345 5.590 11.871 3.775 1.00 46.08 C ATOM 717 SD MET A 345 7.102 11.080 4.441 1.00 50.98 S ATOM 718 CE MET A 345 6.721 9.279 4.354 1.00 52.61 C ATOM 719 C MET A 345 6.187 10.673 0.109 1.00 43.55 C ATOM 720 O MET A 345 6.190 9.427 0.184 1.00 42.43 O ATOM 721 N GLU A 346 5.974 11.311 −1.040 1.00 44.36 N ATOM 722 CA GLU A 346 5.839 10.568 −2.291 1.00 45.64 C ATOM 723 CB GLU A 346 5.107 11.384 −3.339 1.00 46.00 C ATOM 724 CG GLU A 346 3.616 11.455 −3.132 1.00 49.03 C ATOM 725 CD GLU A 346 2.989 12.662 −3.821 1.00 54.25 C ATOM 726 OE1 GLU A 346 3.726 13.555 −4.328 1.00 56.30 O ATOM 727 OE2 GLU A 346 1.740 12.718 −3.852 1.00 58.05 O ATOM 728 C GLU A 346 7.182 10.143 −2.901 1.00 45.79 C ATOM 729 O GLU A 346 7.209 9.327 −3.826 1.00 46.33 O ATOM 730 N LEU A 347 8.288 10.691 −2.411 1.00 45.30 N ATOM 731 CA LEU A 347 9.593 10.361 −2.983 1.00 44.95 C ATOM 732 CB LEU A 347 10.618 11.445 −2.650 1.00 44.65 C ATOM 733 CG LEU A 347 10.252 12.868 −3.077 1.00 44.22 C ATOM 734 CD1 LEU A 347 11.065 13.905 −2.341 1.00 43.57 C ATOM 735 CD2 LEU A 347 10.447 13.049 −4.576 1.00 44.47 C ATOM 736 C LEU A 347 10.086 9.010 −2.469 1.00 44.60 C ATOM 737 O LEU A 347 9.634 8.530 −1.426 1.00 43.99 O ATOM 738 N CYS A 348 11.007 8.392 −3.205 1.00 44.39 N ATOM 739 CA CYS A 348 11.599 7.132 −2.754 1.00 44.78 C ATOM 740 CB CYS A 348 12.511 6.526 −3.835 1.00 44.94 C ATOM 741 SG CYS A 348 13.860 7.612 −4.385 1.00 48.13 S ATOM 742 C CYS A 348 12.388 7.401 −1.474 1.00 43.97 C ATOM 743 O CYS A 348 12.982 8.475 −1.326 1.00 42.90 O ATOM 744 N GLN A 349 12.401 6.427 −0.567 1.00 43.70 N ATOM 745 CA GLN A 349 13.096 6.569 0.708 1.00 44.41 C ATOM 746 CB GLN A 349 13.178 5.250 1.487 1.00 45.15 C ATOM 747 CG GLN A 349 13.587 5.479 2.949 1.00 47.77 C ATOM 748 CD GLN A 349 13.747 4.207 3.723 1.00 51.04 C ATOM 749 OE1 GLN A 349 13.880 3.124 3.139 1.00 53.73 O ATOM 750 NE2 GLN A 349 13.761 4.325 5.040 1.00 53.95 N ATOM 751 C GLN A 349 14.499 7.124 0.495 1.00 43.84 C ATOM 752 O GLN A 349 15.017 7.862 1.324 1.00 43.52 O ATOM 753 N ASN A 350 15.106 6.753 −0.623 1.00 43.26 N ATOM 754 CA ASN A 350 16.451 7.175 −0.929 1.00 43.16 C ATOM 755 CB ASN A 350 16.936 6.460 −2.175 1.00 43.98 C ATOM 756 CG ASN A 350 16.970 4.940 −1.994 1.00 48.26 C ATOM 757 OD1 ASN A 350 18.058 4.340 −1.904 1.00 52.77 O ATOM 758 ND2 ASN A 350 15.773 4.305 −1.934 1.00 51.57 N ATOM 759 C ASN A 350 16.563 8.686 −1.116 1.00 40.98 C ATOM 760 O ASN A 350 17.499 9.296 −0.637 1.00 40.25 O ATOM 761 N ASP A 351 15.638 9.266 −1.860 1.00 39.10 N ATOM 762 CA ASP A 351 15.643 10.696 −2.065 1.00 38.32 C ATOM 763 CB ASP A 351 14.794 11.100 −3.253 1.00 38.60 C ATOM 764 CG ASP A 351 15.504 10.847 −4.590 1.00 41.32 C ATOM 765 OD1 ASP A 351 16.656 10.309 −4.587 1.00 42.06 O ATOM 766 OD2 ASP A 351 14.977 11.143 −5.686 1.00 42.98 O ATOM 767 C ASP A 351 15.194 11.404 −0.783 1.00 36.92 C ATOM 768 O ASP A 351 15.721 12.435 −0.464 1.00 35.52 O ATOM 769 N GLN A 352 14.279 10.813 −0.023 1.00 35.97 N ATOM 770 CA GLN A 352 13.905 11.377 1.265 1.00 35.61 C ATOM 771 CB GLN A 352 12.875 10.478 1.950 1.00 35.48 C ATOM 772 CG GLN A 352 11.497 10.599 1.322 1.00 37.95 C ATOM 773 CD GLN A 352 10.561 9.498 1.737 1.00 40.62 C ATOM 774 OE1 GLN A 352 10.668 8.974 2.839 1.00 40.95 O ATOM 775 NE2 GLN A 352 9.649 9.123 0.848 1.00 44.80 N ATOM 776 C GLN A 352 15.154 11.554 2.137 1.00 34.57 C ATOM 777 O GLN A 352 15.388 12.611 2.720 1.00 32.40 O ATOM 778 N ILE A 353 15.970 10.508 2.184 1.00 33.88 N ATOM 779 CA ILE A 353 17.178 10.487 3.002 1.00 34.01 C ATOM 780 CB ILE A 353 17.772 9.049 2.998 1.00 33.98 C ATOM 781 CG1 ILE A 353 16.805 8.112 3.715 1.00 36.61 C ATOM 782 CD1 ILE A 353 17.075 6.631 3.477 1.00 38.26 C ATOM 783 CG2 ILE A 353 19.101 9.002 3.715 1.00 34.10 C ATOM 784 C ILE A 353 18.225 11.498 2.548 1.00 32.99 C ATOM 785 O ILE A 353 18.821 12.187 3.364 1.00 32.18 O ATOM 786 N VAL A 354 18.466 11.563 1.246 1.00 31.86 N ATOM 787 CA VAL A 354 19.433 12.515 0.698 1.00 31.38 C ATOM 788 CB VAL A 354 19.569 12.320 −0.821 1.00 31.50 C ATOM 789 CG1 VAL A 354 20.148 13.516 −1.458 1.00 31.80 C ATOM 790 CG2 VAL A 354 20.388 11.039 −1.149 1.00 32.45 C ATOM 791 C VAL A 354 19.066 13.988 0.998 1.00 29.81 C ATOM 792 O VAL A 354 19.939 14.794 1.317 1.00 29.46 O ATOM 793 N LEU A 355 17.780 14.316 0.901 1.00 28.52 N ATOM 794 CA LEU A 355 17.317 15.673 1.175 1.00 27.57 C ATOM 795 CB LEU A 355 15.867 15.859 0.755 1.00 27.23 C ATOM 796 CG LEU A 355 15.593 15.830 −0.741 1.00 27.16 C ATOM 797 CD1 LEU A 355 14.104 15.935 −0.931 1.00 28.72 C ATOM 798 CD2 LEU A 355 16.337 16.878 −1.514 1.00 26.89 C ATOM 799 C LEU A 355 17.435 16.028 2.642 1.00 26.38 C ATOM 800 O LEU A 355 17.724 17.171 2.969 1.00 24.91 O ATOM 801 N LEU A 356 17.184 15.067 3.522 1.00 26.87 N ATOM 802 CA LEU A 356 17.330 15.291 4.962 1.00 28.02 C ATOM 803 CB LEU A 356 16.567 14.232 5.788 1.00 28.75 C ATOM 804 CG LEU A 356 15.046 14.442 5.700 1.00 31.27 C ATOM 805 CD1 LEU A 356 14.317 13.319 6.329 1.00 33.71 C ATOM 806 CD2 LEU A 356 14.608 15.740 6.323 1.00 31.98 C ATOM 807 C LEU A 356 18.785 15.340 5.404 1.00 27.73 C ATOM 808 O LEU A 356 19.138 16.160 6.234 1.00 27.81 O ATOM 809 N LYS A 357 19.631 14.463 4.891 1.00 28.00 N ATOM 810 CA LYS A 357 21.038 14.523 5.263 1.00 29.47 C ATOM 811 CB LYS A 357 21.875 13.426 4.613 1.00 29.39 C ATOM 812 CG LYS A 357 21.562 12.033 5.037 1.00 33.92 C ATOM 813 CD LYS A 357 22.586 11.034 4.457 1.00 37.74 C ATOM 814 CE LYS A 357 22.683 9.804 5.331 1.00 41.03 C ATOM 815 NZ LYS A 357 23.255 8.598 4.607 1.00 43.01 N ATOM 816 C LYS A 357 21.600 15.853 4.830 1.00 29.89 C ATOM 817 O LYS A 357 22.382 16.444 5.542 1.00 30.98 O ATOM 818 N ALA A 358 21.207 16.338 3.657 1.00 30.12 N ATOM 819 CA ALA A 358 21.750 17.612 3.181 1.00 30.98 C ATOM 820 CB ALA A 358 21.753 17.654 1.658 1.00 31.73 C ATOM 821 C ALA A 358 21.056 18.857 3.702 1.00 30.81 C ATOM 822 O ALA A 358 21.686 19.893 3.875 1.00 33.30 O ATOM 823 N GLY A 359 19.765 18.777 3.940 1.00 29.32 N ATOM 824 CA GLY A 359 19.040 19.938 4.331 1.00 28.50 C ATOM 825 C GLY A 359 18.606 20.119 5.764 1.00 27.82 C ATOM 826 O GLY A 359 18.236 21.223 6.110 1.00 27.60 O ATOM 827 N SER A 360 18.630 19.089 6.591 1.00 26.28 N ATOM 828 CA SER A 360 18.064 19.239 7.905 1.00 26.79 C ATOM 829 CB SER A 360 17.984 17.889 8.631 1.00 27.01 C ATOM 830 OG SER A 360 19.287 17.372 8.858 1.00 30.95 O ATOM 831 C SER A 360 18.786 20.315 8.699 1.00 26.61 C ATOM 832 O SER A 360 18.139 21.164 9.310 1.00 26.71 O ATOM 833 N LEU A 361 20.116 20.345 8.635 1.00 26.46 N ATOM 834 CA LEU A 361 20.887 21.373 9.338 1.00 26.75 C ATOM 835 CB LEU A 361 22.380 21.042 9.306 1.00 26.79 C ATOM 836 CG LEU A 361 23.250 21.762 10.334 1.00 28.75 C ATOM 837 CD1 LEU A 361 22.803 21.528 11.780 1.00 28.83 C ATOM 838 CD2 LEU A 361 24.747 21.342 10.154 1.00 30.56 C ATOM 839 C LEU A 361 20.660 22.765 8.782 1.00 26.67 C ATOM 840 O LEU A 361 20.593 23.740 9.545 1.00 26.63 O ATOM 841 N GLU A 362 20.550 22.885 7.468 1.00 25.93 N ATOM 842 CA GLU A 362 20.258 24.192 6.875 1.00 26.57 C ATOM 843 CB GLU A 362 20.158 24.122 5.357 1.00 26.98 C ATOM 844 CG GLU A 362 21.329 23.433 4.674 1.00 31.21 C ATOM 845 CD GLU A 362 21.206 23.396 3.149 1.00 37.21 C ATOM 846 OE1 GLU A 362 22.086 22.796 2.478 1.00 41.59 O ATOM 847 OE2 GLU A 362 20.212 23.932 2.619 1.00 43.73 O ATOM 848 C GLU A 362 18.931 24.726 7.430 1.00 25.89 C ATOM 849 O GLU A 362 18.823 25.921 7.697 1.00 24.74 O ATOM 850 N VAL A 363 17.920 23.868 7.592 1.00 25.19 N ATOM 851 CA VAL A 363 16.647 24.362 8.112 1.00 26.09 C ATOM 852 CB VAL A 363 15.494 23.356 7.990 1.00 25.99 C ATOM 853 CG1 VAL A 363 14.256 23.894 8.658 1.00 27.49 C ATOM 854 CG2 VAL A 363 15.182 23.075 6.538 1.00 27.46 C ATOM 855 C VAL A 363 16.815 24.781 9.574 1.00 25.70 C ATOM 856 O VAL A 363 16.210 25.732 10.020 1.00 25.15 O ATOM 857 N VAL A 364 17.682 24.091 10.308 1.00 26.29 N ATOM 858 CA VAL A 364 17.942 24.451 11.690 1.00 25.82 C ATOM 859 CB VAL A 364 18.867 23.435 12.363 1.00 26.43 C ATOM 860 CG1 VAL A 364 19.315 23.910 13.716 1.00 25.43 C ATOM 861 CG2 VAL A 364 18.171 22.105 12.538 1.00 27.04 C ATOM 862 C VAL A 364 18.528 25.865 11.747 1.00 26.05 C ATOM 863 O VAL A 364 18.110 26.692 12.570 1.00 25.23 O ATOM 864 N PHE A 365 19.491 26.162 10.877 1.00 25.43 N ATOM 865 CA PHE A 365 20.098 27.491 10.897 1.00 25.79 C ATOM 866 CB PHE A 365 21.372 27.506 10.102 1.00 26.05 C ATOM 867 CG PHE A 365 22.482 26.755 10.743 1.00 26.79 C ATOM 868 CD1 PHE A 365 22.830 26.990 12.046 1.00 28.32 C ATOM 869 CE1 PHE A 365 23.869 26.329 12.628 1.00 29.90 C ATOM 870 CZ PHE A 365 24.601 25.430 11.894 1.00 31.06 C ATOM 871 CE2 PHE A 365 24.290 25.215 10.614 1.00 30.47 C ATOM 872 CD2 PHE A 365 23.226 25.886 10.024 1.00 29.26 C ATOM 873 C PHE A 365 19.157 28.591 10.418 1.00 26.05 C ATOM 874 O PHE A 365 19.265 29.745 10.846 1.00 26.08 O ATOM 875 N ILE A 366 18.213 28.242 9.554 1.00 26.60 N ATOM 876 CA ILE A 366 17.183 29.194 9.178 1.00 27.03 C ATOM 877 CB ILE A 366 16.365 28.719 7.970 1.00 27.55 C ATOM 878 CG1 ILE A 366 17.273 28.657 6.731 1.00 27.31 C ATOM 879 CD1 ILE A 366 16.641 28.018 5.520 1.00 26.80 C ATOM 880 CG2 ILE A 366 15.179 29.670 7.720 1.00 27.78 C ATOM 881 C ILE A 366 16.325 29.422 10.404 1.00 26.64 C ATOM 882 O ILE A 366 16.186 30.523 10.833 1.00 27.09 O ATOM 883 N ARG A 367 15.792 28.375 11.009 1.00 27.45 N ATOM 884 CA ARG A 367 14.990 28.542 12.229 1.00 27.84 C ATOM 885 CB ARG A 367 14.500 27.204 12.733 1.00 27.21 C ATOM 886 CG ARG A 367 13.501 26.572 11.840 1.00 27.21 C ATOM 887 CD ARG A 367 12.989 25.262 12.377 1.00 26.26 C ATOM 888 NE ARG A 367 11.797 24.825 11.687 1.00 27.92 N ATOM 889 CZ ARG A 367 11.017 23.827 12.095 1.00 30.29 C ATOM 890 NH1 ARG A 367 11.308 23.140 13.190 1.00 30.75 N ATOM 891 NH2 ARG A 367 9.933 23.528 11.412 1.00 31.09 N ATOM 892 C ARG A 367 15.723 29.268 13.367 1.00 28.32 C ATOM 893 O ARG A 367 15.104 29.904 14.228 1.00 28.51 O ATOM 894 N MET A 368 17.038 29.172 13.374 1.00 29.28 N ATOM 895 CA MET A 368 17.832 29.887 14.359 1.00 30.61 C ATOM 896 CB MET A 368 19.311 29.754 14.039 1.00 30.32 C ATOM 897 CG MET A 368 20.188 30.279 15.100 1.00 30.51 C ATOM 898 SD MET A 368 21.905 29.966 14.792 1.00 31.75 S ATOM 899 CE MET A 368 22.107 30.986 13.388 1.00 33.23 C ATOM 900 C MET A 368 17.484 31.372 14.427 1.00 31.27 C ATOM 901 O MET A 368 17.590 31.982 15.481 1.00 31.35 O ATOM 902 N CYS A 369 17.074 31.963 13.328 1.00 32.36 N ATOM 903 CA CYS A 369 16.775 33.385 13.375 1.00 34.85 C ATOM 904 CB CYS A 369 16.614 34.005 11.987 1.00 35.08 C ATOM 905 SG CYS A 369 15.048 33.719 11.195 1.00 41.49 S ATOM 906 C CYS A 369 15.601 33.738 14.286 1.00 34.66 C ATOM 907 O CYS A 369 15.556 34.844 14.785 1.00 36.34 O ATOM 908 N ARG A 370 14.705 32.794 14.569 1.00 33.99 N ATOM 909 CA ARG A 370 13.589 33.045 15.460 1.00 32.77 C ATOM 910 CB ARG A 370 12.559 31.933 15.319 1.00 32.42 C ATOM 911 CG ARG A 370 12.173 31.608 13.890 1.00 32.81 C ATOM 912 CD ARG A 370 11.507 30.270 13.790 1.00 33.89 C ATOM 913 NE ARG A 370 10.153 30.290 14.304 1.00 32.17 N ATOM 914 CZ ARG A 370 9.752 29.738 15.412 1.00 32.53 C ATOM 915 NH1 ARG A 370 10.598 29.098 16.193 1.00 35.61 N ATOM 916 NH2 ARG A 370 8.472 29.815 15.748 1.00 33.49 N ATOM 917 C ARG A 370 14.051 33.036 16.912 1.00 32.83 C ATOM 918 O ARG A 370 13.322 33.465 17.817 1.00 32.92 O ATOM 919 N ALA A 371 15.241 32.488 17.131 1.00 31.07 N ATOM 920 CA ALA A 371 15.757 32.294 18.455 1.00 29.60 C ATOM 921 CB ALA A 371 15.928 30.792 18.720 1.00 29.76 C ATOM 922 C ALA A 371 17.077 33.001 18.554 1.00 28.59 C ATOM 923 O ALA A 371 17.964 32.561 19.226 1.00 27.57 O ATOM 924 N PHE A 372 17.198 34.127 17.888 1.00 28.91 N ATOM 925 CA PHE A 372 18.452 34.836 17.848 1.00 28.90 C ATOM 926 CB PHE A 372 19.079 34.660 16.480 1.00 28.04 C ATOM 927 CG PHE A 372 20.485 35.112 16.406 1.00 27.18 C ATOM 928 CD1 PHE A 372 21.515 34.231 16.614 1.00 28.47 C ATOM 929 CE1 PHE A 372 22.829 34.661 16.546 1.00 30.76 C ATOM 930 CZ PHE A 372 23.107 36.004 16.312 1.00 28.92 C ATOM 931 CE2 PHE A 372 22.085 36.873 16.119 1.00 28.65 C ATOM 932 CD2 PHE A 372 20.781 36.429 16.158 1.00 27.09 C ATOM 933 C PHE A 372 18.202 36.304 18.127 1.00 30.17 C ATOM 934 O PHE A 372 17.312 36.889 17.543 1.00 30.94 O ATOM 935 N ASP A 373 19.005 36.885 19.000 1.00 31.57 N ATOM 936 CA ASP A 373 18.910 38.293 19.376 1.00 33.31 C ATOM 937 CB ASP A 373 19.058 38.438 20.900 1.00 33.82 C ATOM 938 CG ASP A 373 18.989 39.902 21.381 1.00 36.02 C ATOM 939 OD1 ASP A 373 18.985 40.818 20.530 1.00 41.04 O ATOM 940 OD2 ASP A 373 18.972 40.227 22.591 1.00 36.84 O ATOM 941 C ASP A 373 20.020 39.049 18.649 1.00 34.95 C ATOM 942 O ASP A 373 21.198 39.063 19.064 1.00 34.64 O ATOM 943 N SER A 374 19.636 39.678 17.553 1.00 36.75 N ATOM 944 CA SER A 374 20.585 40.409 16.717 1.00 39.28 C ATOM 945 CB SER A 374 19.866 40.916 15.474 1.00 39.26 C ATOM 946 OG SER A 374 20.836 41.201 14.487 1.00 43.88 O ATOM 947 C SER A 374 21.325 41.581 17.378 1.00 39.94 C ATOM 948 O SER A 374 22.515 41.766 17.173 1.00 40.56 O ATOM 949 N GLN A 375 20.626 42.366 18.186 1.00 41.01 N ATOM 950 CA GLN A 375 21.239 43.516 18.810 1.00 41.65 C ATOM 951 CB GLN A 375 20.197 44.362 19.565 1.00 42.91 C ATOM 952 CG GLN A 375 18.913 44.675 18.767 1.00 47.27 C ATOM 953 CD GLN A 375 18.116 45.864 19.353 1.00 53.49 C ATOM 954 OE1 GLN A 375 18.626 46.997 19.399 1.00 57.17 O ATOM 955 NE2 GLN A 375 16.877 45.608 19.788 1.00 54.72 N ATOM 956 C GLN A 375 22.344 43.098 19.762 1.00 40.86 C ATOM 957 O GLN A 375 23.365 43.773 19.858 1.00 41.50 O ATOM 958 N ASN A 376 22.155 41.987 20.463 1.00 39.20 N ATOM 959 CA ASN A 376 23.137 41.552 21.441 1.00 38.16 C ATOM 960 CB ASN A 376 22.438 41.264 22.766 1.00 38.40 C ATOM 961 CG ASN A 376 21.791 42.527 23.387 1.00 40.33 C ATOM 962 OD1 ASN A 376 22.488 43.368 23.935 1.00 41.58 O ATOM 963 ND2 ASN A 376 20.452 42.644 23.301 1.00 40.49 N ATOM 964 C ASN A 376 24.019 40.360 21.002 1.00 36.51 C ATOM 965 O ASN A 376 24.852 39.906 21.769 1.00 37.34 O ATOM 966 N ASN A 377 23.840 39.859 19.789 1.00 33.92 N ATOM 967 CA ASN A 377 24.632 38.727 19.284 1.00 32.39 C ATOM 968 CB ASN A 377 26.094 39.138 19.079 1.00 31.52 C ATOM 969 CG ASN A 377 26.772 38.334 17.993 1.00 31.73 C ATOM 970 OD1 ASN A 377 26.142 37.995 16.998 1.00 33.03 O ATOM 971 ND2 ASN A 377 28.050 38.007 18.176 1.00 27.90 N ATOM 972 C ASN A 377 24.550 37.477 20.194 1.00 31.00 C ATOM 973 O ASN A 377 25.560 37.005 20.708 1.00 31.17 O ATOM 974 N THR A 378 23.336 36.976 20.410 1.00 29.28 N ATOM 975 CA THR A 378 23.110 35.831 21.282 1.00 28.19 C ATOM 976 CB THR A 378 22.643 36.241 22.727 1.00 29.06 C ATOM 977 OG1 THR A 378 21.395 36.949 22.674 1.00 27.46 O ATOM 978 CG2 THR A 378 23.663 37.127 23.462 1.00 28.26 C ATOM 979 C THR A 378 22.070 34.895 20.708 1.00 26.71 C ATOM 980 O THR A 378 21.139 35.318 20.011 1.00 26.15 O ATOM 981 N VAL A 379 22.231 33.615 21.032 1.00 26.22 N ATOM 982 CA VAL A 379 21.361 32.557 20.517 1.00 24.86 C ATOM 983 CB VAL A 379 22.149 31.671 19.525 1.00 24.33 C ATOM 984 CG1 VAL A 379 23.217 30.881 20.210 1.00 24.14 C ATOM 985 CG2 VAL A 379 21.210 30.747 18.777 1.00 24.47 C ATOM 986 C VAL A 379 20.815 31.711 21.637 1.00 24.23 C ATOM 987 O VAL A 379 21.507 31.421 22.559 1.00 24.32 O ATOM 988 N TYR A 380 19.569 31.283 21.519 1.00 24.94 N ATOM 989 CA TYR A 380 18.905 30.450 22.506 1.00 25.03 C ATOM 990 CB TYR A 380 17.410 30.313 22.141 1.00 24.86 C ATOM 991 CG TYR A 380 16.514 29.758 23.215 1.00 27.20 C ATOM 992 CD1 TYR A 380 16.614 30.197 24.535 1.00 32.61 C ATOM 993 CE1 TYR A 380 15.799 29.705 25.521 1.00 32.61 C ATOM 994 CZ TYR A 380 14.852 28.746 25.210 1.00 35.82 C ATOM 995 OH TYR A 380 14.038 28.236 26.193 1.00 38.69 O ATOM 996 CE2 TYR A 380 14.742 28.277 23.938 1.00 34.16 C ATOM 997 CD2 TYR A 380 15.589 28.791 22.939 1.00 32.66 C ATOM 998 C TYR A 380 19.589 29.086 22.523 1.00 25.13 C ATOM 999 O TYR A 380 19.647 28.416 21.514 1.00 25.44 O ATOM 1000 N PHE A 381 20.127 28.698 23.675 1.00 25.96 N ATOM 1001 CA PHE A 381 20.902 27.470 23.824 1.00 25.59 C ATOM 1002 CB PHE A 381 22.328 27.773 23.471 1.00 25.60 C ATOM 1003 CG PHE A 381 23.263 26.709 23.828 1.00 25.28 C ATOM 1004 CD1 PHE A 381 23.306 25.561 23.106 1.00 26.68 C ATOM 1005 CE1 PHE A 381 24.190 24.559 23.454 1.00 29.89 C ATOM 1006 CZ PHE A 381 25.049 24.733 24.537 1.00 28.60 C ATOM 1007 CE2 PHE A 381 25.007 25.865 25.234 1.00 28.13 C ATOM 1008 CD2 PHE A 381 24.107 26.851 24.895 1.00 27.85 C ATOM 1009 C PHE A 381 20.879 26.914 25.251 1.00 26.62 C ATOM 1010 O PHE A 381 21.215 27.604 26.209 1.00 26.25 O ATOM 1011 N ASP A 382 20.481 25.664 25.416 1.00 27.37 N ATOM 1012 CA ASP A 382 20.441 25.075 26.766 1.00 28.62 C ATOM 1013 CB ASP A 382 21.885 24.760 27.242 1.00 28.80 C ATOM 1014 CG ASP A 382 21.936 23.653 28.283 1.00 31.74 C ATOM 1015 OD1 ASP A 382 20.973 22.859 28.374 1.00 34.71 O ATOM 1016 OD2 ASP A 382 22.911 23.477 29.045 1.00 34.98 O ATOM 1017 C ASP A 382 19.705 25.888 27.853 1.00 28.15 C ATOM 1018 O ASP A 382 20.150 25.923 28.997 1.00 29.36 O ATOM 1019 N GLY A 383 18.564 26.485 27.514 1.00 28.44 N ATOM 1020 CA GLY A 383 17.770 27.238 28.488 1.00 28.32 C ATOM 1021 C GLY A 383 17.958 28.758 28.594 1.00 27.86 C ATOM 1022 O GLY A 383 17.144 29.476 29.196 1.00 29.11 O ATOM 1023 N LYS A 384 19.032 29.289 28.033 1.00 26.62 N ATOM 1024 CA LYS A 384 19.241 30.731 28.108 1.00 26.42 C ATOM 1025 CB LYS A 384 20.185 31.068 29.267 1.00 26.08 C ATOM 1026 CG LYS A 384 19.627 30.747 30.653 1.00 28.51 C ATOM 1027 CD LYS A 384 20.486 31.424 31.751 1.00 29.39 C ATOM 1028 CE LYS A 384 20.028 31.086 33.196 1.00 30.70 C ATOM 1029 NZ LYS A 384 20.910 31.746 34.288 1.00 29.22 N ATOM 1030 C LYS A 384 19.797 31.259 26.791 1.00 25.94 C ATOM 1031 O LYS A 384 20.097 30.466 25.900 1.00 26.76 O ATOM 1032 N TYR A 385 19.974 32.578 26.672 1.00 24.63 N ATOM 1033 CA TYR A 385 20.572 33.145 25.466 1.00 24.57 C ATOM 1034 CB TYR A 385 19.948 34.488 25.115 1.00 24.03 C ATOM 1035 CG TYR A 385 18.685 34.353 24.311 1.00 24.39 C ATOM 1036 CD1 TYR A 385 17.468 34.095 24.917 1.00 26.02 C ATOM 1037 CE1 TYR A 385 16.320 34.000 24.163 1.00 26.31 C ATOM 1038 CZ TYR A 385 16.411 34.121 22.799 1.00 28.74 C ATOM 1039 OH TYR A 385 15.321 33.976 21.988 1.00 27.24 O ATOM 1040 CE2 TYR A 385 17.628 34.353 22.195 1.00 26.89 C ATOM 1041 CD2 TYR A 385 18.723 34.458 22.944 1.00 24.65 C ATOM 1042 C TYR A 385 22.101 33.213 25.671 1.00 24.69 C ATOM 1043 O TYR A 385 22.590 33.626 26.720 1.00 25.62 O ATOM 1044 N ALA A 386 22.825 32.741 24.671 1.00 24.40 N ATOM 1045 CA ALA A 386 24.254 32.515 24.738 1.00 24.38 C ATOM 1046 CB ALA A 386 24.514 31.107 24.385 1.00 23.79 C ATOM 1047 C ALA A 386 25.008 33.368 23.745 1.00 25.29 C ATOM 1048 O ALA A 386 24.623 33.438 22.579 1.00 26.61 O ATOM 1049 N SER A 387 26.085 33.976 24.209 1.00 25.98 N ATOM 1050 CA SER A 387 27.031 34.711 23.369 1.00 26.98 C ATOM 1051 CB SER A 387 27.840 35.628 24.236 1.00 26.78 C ATOM 1052 OG SER A 387 28.416 34.847 25.267 1.00 30.72 O ATOM 1053 C SER A 387 27.985 33.696 22.787 1.00 27.67 C ATOM 1054 O SER A 387 27.984 32.548 23.233 1.00 26.96 O ATOM 1055 N PRO A 388 28.776 34.084 21.785 1.00 28.55 N ATOM 1056 CA PRO A 388 29.788 33.193 21.216 1.00 29.40 C ATOM 1057 CB PRO A 388 30.510 34.088 20.180 1.00 29.67 C ATOM 1058 CG PRO A 388 29.538 35.118 19.839 1.00 29.41 C ATOM 1059 CD PRO A 388 28.781 35.393 21.107 1.00 29.03 C ATOM 1060 C PRO A 388 30.775 32.659 22.250 1.00 30.29 C ATOM 1061 O PRO A 388 31.346 31.581 22.052 1.00 30.55 O ATOM 1062 N ASP A 389 30.972 33.389 23.338 1.00 31.61 N ATOM 1063 CA ASP A 389 31.864 32.951 24.406 1.00 32.74 C ATOM 1064 CB ASP A 389 31.882 33.986 25.510 1.00 34.07 C ATOM 1065 CG ASP A 389 32.640 35.207 25.127 1.00 39.93 C ATOM 1066 OD1 ASP A 389 33.325 35.175 24.070 1.00 47.04 O ATOM 1067 OD2 ASP A 389 32.601 36.259 25.813 1.00 46.60 O ATOM 1068 C ASP A 389 31.484 31.614 25.044 1.00 31.53 C ATOM 1069 O ASP A 389 32.359 30.893 25.528 1.00 31.63 O ATOM 1070 N VAL A 390 30.189 31.317 25.069 1.00 29.87 N ATOM 1071 CA VAL A 390 29.667 30.079 25.616 1.00 29.20 C ATOM 1072 CB VAL A 390 28.119 30.083 25.572 1.00 29.33 C ATOM 1073 CG1 VAL A 390 27.579 28.705 25.643 1.00 29.50 C ATOM 1074 CG2 VAL A 390 27.582 30.907 26.704 1.00 29.08 C ATOM 1075 C VAL A 390 30.183 28.865 24.870 1.00 28.35 C ATOM 1076 O VAL A 390 30.307 27.811 25.440 1.00 28.58 O ATOM 1077 N PHE A 391 30.551 29.038 23.610 1.00 28.30 N ATOM 1078 CA PHE A 391 31.038 27.943 22.785 1.00 27.98 C ATOM 1079 CB PHE A 391 30.365 28.034 21.431 1.00 27.73 C ATOM 1080 CG PHE A 391 28.882 28.039 21.514 1.00 26.60 C ATOM 1081 CD1 PHE A 391 28.180 29.233 21.549 1.00 25.13 C ATOM 1082 CE1 PHE A 391 26.814 29.228 21.640 1.00 24.90 C ATOM 1083 CZ PHE A 391 26.129 28.025 21.674 1.00 24.94 C ATOM 1084 CE2 PHE A 391 26.812 26.837 21.650 1.00 24.26 C ATOM 1085 CD2 PHE A 391 28.180 26.840 21.574 1.00 25.61 C ATOM 1086 C PHE A 391 32.566 27.838 22.571 1.00 28.31 C ATOM 1087 O PHE A 391 33.018 27.054 21.729 1.00 27.05 O ATOM 1088 N LYS A 392 33.328 28.579 23.356 1.00 29.26 N ATOM 1089 CA LYS A 392 34.795 28.578 23.281 1.00 31.34 C ATOM 1090 CB LYS A 392 35.366 29.495 24.377 1.00 32.61 C ATOM 1091 CG LYS A 392 36.861 29.771 24.281 1.00 35.79 C ATOM 1092 CD LYS A 392 37.301 30.620 25.474 1.00 39.49 C ATOM 1093 CE LYS A 392 38.826 30.579 25.699 1.00 41.94 C ATOM 1094 NZ LYS A 392 39.185 31.071 27.075 1.00 42.28 N ATOM 1095 C LYS A 392 35.456 27.202 23.366 1.00 31.54 C ATOM 1096 O LYS A 392 36.322 26.898 22.567 1.00 31.50 O ATOM 1097 N SER A 393 35.008 26.343 24.288 1.00 32.67 N ATOM 1098 CA SER A 393 35.571 25.003 24.431 1.00 32.44 C ATOM 1099 CB SER A 393 34.989 24.270 25.624 1.00 32.78 C ATOM 1100 OG SER A 393 35.056 25.069 26.784 1.00 35.03 O ATOM 1101 C SER A 393 35.400 24.110 23.240 1.00 32.29 C ATOM 1102 O SER A 393 36.048 23.062 23.169 1.00 32.31 O ATOM 1103 N LEU A 394 34.534 24.465 22.303 1.00 32.26 N ATOM 1104 CA LEU A 394 34.436 23.653 21.121 1.00 31.95 C ATOM 1105 CB LEU A 394 33.304 24.091 20.195 1.00 32.22 C ATOM 1106 CG LEU A 394 31.829 23.898 20.560 1.00 30.03 C ATOM 1107 CD1 LEU A 394 30.964 24.445 19.463 1.00 27.50 C ATOM 1108 CD2 LEU A 394 31.547 22.458 20.809 1.00 31.13 C ATOM 1109 C LEU A 394 35.720 23.720 20.316 1.00 32.56 C ATOM 1110 O LEU A 394 35.948 22.892 19.493 1.00 32.76 O ATOM 1111 N GLY A 395 36.520 24.749 20.498 1.00 35.25 N ATOM 1112 CA GLY A 395 37.717 24.928 19.696 1.00 36.37 C ATOM 1113 C GLY A 395 37.426 25.284 18.243 1.00 37.83 C ATOM 1114 O GLY A 395 38.249 24.980 17.367 1.00 38.76 O ATOM 1115 N CYS A 396 36.300 25.969 17.988 1.00 38.87 N ATOM 1116 CA CYS A 396 35.877 26.363 16.626 1.00 39.61 C ATOM 1117 CB CYS A 396 34.603 25.638 16.231 1.00 40.04 C ATOM 1118 SG CYS A 396 34.493 23.892 16.532 1.00 47.12 S ATOM 1119 C CYS A 396 35.483 27.836 16.522 1.00 38.76 C ATOM 1120 O CYS A 396 34.364 28.140 16.063 1.00 37.44 O ATOM 1121 N GLU A 397 36.359 28.747 16.928 1.00 38.45 N ATOM 1122 CA GLU A 397 35.995 30.158 16.905 1.00 39.15 C ATOM 1123 CB GLU A 397 37.123 31.064 17.392 1.00 39.98 C ATOM 1124 CG GLU A 397 37.786 30.611 18.702 1.00 45.20 C ATOM 1125 CD GLU A 397 37.249 31.254 19.991 1.00 51.31 C ATOM 1126 OE1 GLU A 397 36.045 31.041 20.323 1.00 55.26 O ATOM 1127 OE2 GLU A 397 38.046 31.920 20.717 1.00 53.17 O ATOM 1128 C GLU A 397 35.487 30.605 15.520 1.00 37.80 C ATOM 1129 O GLU A 397 34.511 31.296 15.465 1.00 37.56 O ATOM 1130 N ASP A 398 36.118 30.197 14.423 1.00 37.26 N ATOM 1131 CA ASP A 398 35.685 30.640 13.091 1.00 37.80 C ATOM 1132 CB ASP A 398 36.695 30.253 12.000 1.00 39.29 C ATOM 1133 CG ASP A 398 38.008 31.019 12.097 1.00 42.86 C ATOM 1134 OD1 ASP A 398 38.097 32.024 12.844 1.00 48.94 O ATOM 1135 OD2 ASP A 398 39.018 30.660 11.450 1.00 47.39 O ATOM 1136 C ASP A 398 34.305 30.103 12.676 1.00 35.53 C ATOM 1137 O ASP A 398 33.472 30.848 12.182 1.00 35.67 O ATOM 1138 N PHE A 399 34.075 28.814 12.852 1.00 33.02 N ATOM 1139 CA PHE A 399 32.755 28.264 12.574 1.00 31.62 C ATOM 1140 CB PHE A 399 32.757 26.754 12.735 1.00 31.05 C ATOM 1141 CG PHE A 399 31.399 26.151 12.729 1.00 30.78 C ATOM 1142 CD1 PHE A 399 30.702 26.027 11.567 1.00 30.86 C ATOM 1143 CE1 PHE A 399 29.437 25.502 11.561 1.00 31.41 C ATOM 1144 CZ PHE A 399 28.856 25.092 12.742 1.00 31.17 C ATOM 1145 CE2 PHE A 399 29.526 25.243 13.905 1.00 30.20 C ATOM 1146 CD2 PHE A 399 30.797 25.777 13.906 1.00 29.57 C ATOM 1147 C PHE A 399 31.665 28.932 13.466 1.00 30.38 C ATOM 1148 O PHE A 399 30.567 29.240 13.014 1.00 30.06 O ATOM 1149 N ILE A 400 31.975 29.187 14.718 1.00 29.09 N ATOM 1150 CA ILE A 400 30.988 29.793 15.584 1.00 28.21 C ATOM 1151 CB ILE A 400 31.453 29.709 17.022 1.00 27.49 C ATOM 1152 CG1 ILE A 400 31.426 28.255 17.501 1.00 28.01 C ATOM 1153 CD1 ILE A 400 30.013 27.629 17.525 1.00 27.35 C ATOM 1154 CG2 ILE A 400 30.557 30.501 17.930 1.00 28.61 C ATOM 1155 C ILE A 400 30.717 31.213 15.132 1.00 28.30 C ATOM 1156 O ILE A 400 29.538 31.652 15.105 1.00 27.29 O ATOM 1157 N SER A 401 31.774 31.949 14.758 1.00 27.64 N ATOM 1158 CA SER A 401 31.552 33.329 14.298 1.00 28.85 C ATOM 1159 CB SER A 401 32.850 34.152 14.224 1.00 28.93 C ATOM 1160 OG SER A 401 33.622 33.761 13.129 1.00 35.10 O ATOM 1161 C SER A 401 30.736 33.397 12.997 1.00 27.77 C ATOM 1162 O SER A 401 29.938 34.283 12.818 1.00 28.99 O ATOM 1163 N PHE A 402 30.910 32.423 12.133 1.00 27.14 N ATOM 1164 CA PHE A 402 30.144 32.276 10.923 1.00 27.41 C ATOM 1165 CB PHE A 402 30.800 31.145 10.137 1.00 27.67 C ATOM 1166 CG PHE A 402 30.303 30.940 8.733 1.00 30.03 C ATOM 1167 CD1 PHE A 402 29.486 31.840 8.091 1.00 31.94 C ATOM 1168 CE1 PHE A 402 29.061 31.618 6.813 1.00 30.13 C ATOM 1169 CZ PHE A 402 29.438 30.512 6.124 1.00 30.57 C ATOM 1170 CE2 PHE A 402 30.266 29.595 6.712 1.00 33.09 C ATOM 1171 CD2 PHE A 402 30.704 29.815 8.030 1.00 34.00 C ATOM 1172 C PHE A 402 28.657 31.992 11.290 1.00 26.84 C ATOM 1173 O PHE A 402 27.733 32.571 10.717 1.00 25.94 O ATOM 1174 N VAL A 403 28.416 31.141 12.280 1.00 26.02 N ATOM 1175 CA VAL A 403 27.035 30.855 12.669 1.00 25.17 C ATOM 1176 CB VAL A 403 26.967 29.787 13.797 1.00 24.18 C ATOM 1177 CG1 VAL A 403 25.606 29.750 14.394 1.00 25.35 C ATOM 1178 CG2 VAL A 403 27.294 28.446 13.255 1.00 24.23 C ATOM 1179 C VAL A 403 26.339 32.131 13.158 1.00 24.80 C ATOM 1180 O VAL A 403 25.194 32.422 12.831 1.00 24.70 O ATOM 1181 N PHE A 404 27.011 32.868 13.998 1.00 24.99 N ATOM 1182 CA PHE A 404 26.398 34.058 14.547 1.00 25.96 C ATOM 1183 CB PHE A 404 27.212 34.579 15.719 1.00 26.02 C ATOM 1184 CG PHE A 404 26.912 33.880 17.037 1.00 25.96 C ATOM 1185 CD1 PHE A 404 27.378 32.614 17.296 1.00 26.60 C ATOM 1186 CE1 PHE A 404 27.087 31.962 18.535 1.00 27.71 C ATOM 1187 CZ PHE A 404 26.358 32.572 19.475 1.00 26.31 C ATOM 1188 CE2 PHE A 404 25.881 33.846 19.230 1.00 29.49 C ATOM 1189 CD2 PHE A 404 26.178 34.501 18.010 1.00 28.52 C ATOM 1190 C PHE A 404 26.232 35.121 13.488 1.00 26.66 C ATOM 1191 O PHE A 404 25.278 35.891 13.515 1.00 27.41 O ATOM 1192 N GLU A 405 27.151 35.166 12.537 1.00 27.79 N ATOM 1193 CA GLU A 405 27.078 36.165 11.487 1.00 27.80 C ATOM 1194 CB GLU A 405 28.339 36.163 10.623 1.00 28.35 C ATOM 1195 CG GLU A 405 28.147 37.016 9.384 1.00 31.23 C ATOM 1196 CD GLU A 405 29.446 37.528 8.769 1.00 35.82 C ATOM 1197 OE1 GLU A 405 30.552 37.009 9.096 1.00 37.08 O ATOM 1198 OE2 GLU A 405 29.334 38.448 7.937 1.00 35.95 O ATOM 1199 C GLU A 405 25.861 35.864 10.629 1.00 27.96 C ATOM 1200 O GLU A 405 25.126 36.773 10.228 1.00 25.82 O ATOM 1201 N PHE A 406 25.658 34.576 10.373 1.00 27.97 N ATOM 1202 CA PHE A 406 24.508 34.148 9.629 1.00 29.23 C ATOM 1203 CB PHE A 406 24.549 32.656 9.326 1.00 28.50 C ATOM 1204 CG PHE A 406 23.459 32.229 8.434 1.00 29.33 C ATOM 1205 CD1 PHE A 406 23.588 32.396 7.058 1.00 31.26 C ATOM 1206 CE1 PHE A 406 22.574 32.049 6.214 1.00 29.99 C ATOM 1207 CZ PHE A 406 21.389 31.531 6.737 1.00 30.86 C ATOM 1208 CE2 PHE A 406 21.253 31.340 8.104 1.00 30.00 C ATOM 1209 CD2 PHE A 406 22.277 31.698 8.949 1.00 27.04 C ATOM 1210 C PHE A 406 23.204 34.511 10.367 1.00 30.08 C ATOM 1211 O PHE A 406 22.238 34.936 9.746 1.00 29.57 O ATOM 1212 N GLY A 407 23.186 34.337 11.681 1.00 31.28 N ATOM 1213 CA GLY A 407 22.009 34.643 12.485 1.00 31.96 C ATOM 1214 C GLY A 407 21.699 36.116 12.401 1.00 33.32 C ATOM 1215 O GLY A 407 20.581 36.539 12.135 1.00 32.80 O ATOM 1216 N LYS A 408 22.729 36.915 12.577 1.00 35.20 N ATOM 1217 CA LYS A 408 22.586 38.344 12.430 1.00 36.71 C ATOM 1218 CB LYS A 408 23.931 38.993 12.688 1.00 37.55 C ATOM 1219 CG LYS A 408 23.845 40.473 12.958 1.00 40.89 C ATOM 1220 CD LYS A 408 25.125 41.000 13.605 1.00 44.55 C ATOM 1221 CE LYS A 408 25.143 40.750 15.121 1.00 46.16 C ATOM 1222 NZ LYS A 408 26.310 41.466 15.786 1.00 47.26 N ATOM 1223 C LYS A 408 22.090 38.756 11.033 1.00 37.33 C ATOM 1224 O LYS A 408 21.233 39.637 10.881 1.00 37.08 O ATOM 1225 N SER A 409 22.610 38.106 10.005 1.00 37.62 N ATOM 1226 CA SER A 409 22.258 38.499 8.649 1.00 38.03 C ATOM 1227 CB SER A 409 23.258 37.906 7.681 1.00 37.87 C ATOM 1228 OG SER A 409 22.671 37.759 6.421 1.00 43.04 O ATOM 1229 C SER A 409 20.816 38.139 8.273 1.00 37.59 C ATOM 1230 O SER A 409 20.146 38.891 7.596 1.00 37.65 O ATOM 1231 N LEU A 410 20.330 36.994 8.730 1.00 38.00 N ATOM 1232 CA LEU A 410 18.944 36.599 8.476 1.00 38.06 C ATOM 1233 CB LEU A 410 18.771 35.108 8.728 1.00 37.93 C ATOM 1234 CG LEU A 410 17.711 34.363 7.930 1.00 39.48 C ATOM 1235 CD1 LEU A 410 17.866 34.566 6.431 1.00 40.64 C ATOM 1236 CD2 LEU A 410 17.795 32.873 8.280 1.00 39.84 C ATOM 1237 C LEU A 410 17.969 37.447 9.323 1.00 37.89 C ATOM 1238 O LEU A 410 16.907 37.826 8.859 1.00 36.02 O ATOM 1239 N CYS A 411 18.344 37.745 10.558 1.00 39.15 N ATOM 1240 CA CYS A 411 17.552 38.634 11.416 1.00 40.62 C ATOM 1241 CB CYS A 411 18.243 38.819 12.753 1.00 41.09 C ATOM 1242 SG CYS A 411 18.069 37.449 13.893 1.00 41.89 S ATOM 1243 C CYS A 411 17.371 40.029 10.822 1.00 41.43 C ATOM 1244 O CYS A 411 16.301 40.596 10.880 1.00 41.63 O ATOM 1245 N SER A 412 18.433 40.579 10.253 1.00 42.39 N ATOM 1246 CA SER A 412 18.381 41.897 9.641 1.00 43.17 C ATOM 1247 CB SER A 412 19.756 42.278 9.067 1.00 42.83 C ATOM 1248 OG SER A 412 19.897 41.811 7.730 1.00 43.89 O ATOM 1249 C SER A 412 17.325 42.003 8.534 1.00 44.19 C ATOM 1250 O SER A 412 17.030 43.119 8.072 1.00 45.40 O ATOM 1251 N MET A 413 16.771 40.880 8.085 1.00 43.86 N ATOM 1252 CA MET A 413 15.732 40.913 7.065 1.00 44.53 C ATOM 1253 CB MET A 413 15.874 39.740 6.102 1.00 44.68 C ATOM 1254 CG MET A 413 17.179 39.724 5.375 1.00 45.77 C ATOM 1255 SD MET A 413 17.293 38.227 4.484 1.00 52.29 S ATOM 1256 CE MET A 413 19.021 38.123 4.084 1.00 52.15 C ATOM 1257 C MET A 413 14.319 40.920 7.666 1.00 44.82 C ATOM 1258 O MET A 413 13.354 41.154 6.948 1.00 45.27 O ATOM 1259 N HIS A 414 14.207 40.686 8.969 1.00 44.42 N ATOM 1260 CA HIS A 414 12.917 40.694 9.651 1.00 45.37 C ATOM 1261 CB HIS A 414 12.369 42.124 9.831 1.00 46.54 C ATOM 1262 CG HIS A 414 13.414 43.131 10.202 1.00 49.03 C ATOM 1263 ND1 HIS A 414 13.905 43.252 11.484 1.00 52.00 N ATOM 1264 CE1 HIS A 414 14.830 44.198 11.511 1.00 52.74 C ATOM 1265 NE2 HIS A 414 14.956 44.694 10.290 1.00 53.78 N ATOM 1266 CD2 HIS A 414 14.078 44.046 9.452 1.00 51.02 C ATOM 1267 C HIS A 414 11.920 39.867 8.867 1.00 44.54 C ATOM 1268 O HIS A 414 10.905 40.380 8.397 1.00 45.13 O ATOM 1269 N LEU A 415 12.221 38.586 8.712 1.00 43.37 N ATOM 1270 CA LEU A 415 11.345 37.696 7.992 1.00 42.05 C ATOM 1271 CB LEU A 415 12.098 36.448 7.563 1.00 42.25 C ATOM 1272 CG LEU A 415 13.274 36.739 6.635 1.00 42.37 C ATOM 1273 CD1 LEU A 415 14.213 35.584 6.615 1.00 43.50 C ATOM 1274 CD2 LEU A 415 12.736 37.013 5.254 1.00 42.77 C ATOM 1275 C LEU A 415 10.200 37.311 8.889 1.00 41.21 C ATOM 1276 O LEU A 415 10.379 37.116 10.073 1.00 40.43 O ATOM 1277 N THR A 416 9.019 37.191 8.310 1.00 40.22 N ATOM 1278 CA THR A 416 7.852 36.771 9.050 1.00 39.80 C ATOM 1279 CB THR A 416 6.587 37.152 8.269 1.00 39.84 C ATOM 1280 OG1 THR A 416 6.623 36.538 6.978 1.00 39.74 O ATOM 1281 CG2 THR A 416 6.546 38.636 7.950 1.00 39.98 C ATOM 1282 C THR A 416 7.890 35.270 9.203 1.00 39.01 C ATOM 1283 O THR A 416 8.698 34.609 8.553 1.00 38.71 O ATOM 1284 N GLU A 417 7.004 34.728 10.035 1.00 38.46 N ATOM 1285 CA GLU A 417 6.925 33.289 10.241 1.00 38.70 C ATOM 1286 CB GLU A 417 5.879 32.940 11.318 1.00 38.85 C ATOM 1287 CG GLU A 417 6.350 33.068 12.768 1.00 41.11 C ATOM 1288 CD GLU A 417 7.583 32.225 13.115 1.00 41.56 C ATOM 1289 OE1 GLU A 417 7.436 31.070 13.527 1.00 40.66 O ATOM 1290 OE2 GLU A 417 8.707 32.744 13.014 1.00 44.69 O ATOM 1291 C GLU A 417 6.599 32.558 8.921 1.00 38.40 C ATOM 1292 O GLU A 417 7.140 31.493 8.629 1.00 37.21 O ATOM 1293 N ASP A 418 5.717 33.122 8.117 1.00 38.52 N ATOM 1294 CA ASP A 418 5.382 32.489 6.845 1.00 39.36 C ATOM 1295 CB ASP A 418 4.134 33.115 6.221 1.00 40.08 C ATOM 1296 CG ASP A 418 2.858 32.783 7.007 1.00 44.36 C ATOM 1297 OD1 ASP A 418 2.931 31.961 7.953 1.00 50.10 O ATOM 1298 OD2 ASP A 418 1.736 33.282 6.742 1.00 48.86 O ATOM 1299 C ASP A 418 6.540 32.531 5.865 1.00 38.10 C ATOM 1300 O ASP A 418 6.712 31.634 5.057 1.00 37.14 O ATOM 1301 N GLU A 419 7.311 33.602 5.925 1.00 37.67 N ATOM 1302 CA GLU A 419 8.479 33.730 5.074 1.00 37.99 C ATOM 1303 CB GLU A 419 9.062 35.165 5.163 1.00 38.22 C ATOM 1304 CG GLU A 419 8.269 36.175 4.336 1.00 40.90 C ATOM 1305 CD GLU A 419 8.530 37.629 4.682 1.00 41.76 C ATOM 1306 OE1 GLU A 419 9.193 37.895 5.685 1.00 43.26 O ATOM 1307 OE2 GLU A 419 8.059 38.512 3.938 1.00 45.04 O ATOM 1308 C GLU A 419 9.519 32.657 5.459 1.00 36.84 C ATOM 1309 O GLU A 419 10.106 32.012 4.590 1.00 36.16 O ATOM 1310 N ILE A 420 9.708 32.453 6.760 1.00 35.93 N ATOM 1311 CA ILE A 420 10.695 31.488 7.233 1.00 35.74 C ATOM 1312 CB ILE A 420 10.899 31.607 8.740 1.00 36.17 C ATOM 1313 CG1 ILE A 420 11.712 32.873 9.008 1.00 38.07 C ATOM 1314 CD1 ILE A 420 11.838 33.228 10.464 1.00 39.66 C ATOM 1315 CG2 ILE A 420 11.617 30.377 9.287 1.00 36.15 C ATOM 1316 C ILE A 420 10.311 30.085 6.856 1.00 34.34 C ATOM 1317 O ILE A 420 11.156 29.282 6.517 1.00 33.17 O ATOM 1318 N ALA A 421 9.013 29.813 6.914 1.00 33.91 N ATOM 1319 CA ALA A 421 8.459 28.535 6.558 1.00 32.70 C ATOM 1320 CB ALA A 421 7.024 28.543 6.813 1.00 33.68 C ATOM 1321 C ALA A 421 8.676 28.194 5.084 1.00 32.56 C ATOM 1322 O ALA A 421 9.065 27.064 4.769 1.00 31.53 O ATOM 1323 N LEU A 422 8.384 29.140 4.188 1.00 31.71 N ATOM 1324 CA LEU A 422 8.508 28.871 2.773 1.00 32.27 C ATOM 1325 CB LEU A 422 7.779 29.923 1.948 1.00 33.13 C ATOM 1326 CG LEU A 422 6.261 29.927 2.141 1.00 37.47 C ATOM 1327 CD1 LEU A 422 5.611 30.995 1.361 1.00 40.39 C ATOM 1328 CD2 LEU A 422 5.677 28.631 1.696 1.00 40.84 C ATOM 1329 C LEU A 422 9.972 28.770 2.367 1.00 31.63 C ATOM 1330 O LEU A 422 10.319 28.037 1.452 1.00 31.16 O ATOM 1331 N PHE A 423 10.828 29.525 3.046 1.00 31.46 N ATOM 1332 CA PHE A 423 12.247 29.487 2.758 1.00 31.86 C ATOM 1333 CB PHE A 423 12.957 30.654 3.414 1.00 32.18 C ATOM 1334 CG PHE A 423 14.396 30.795 3.015 1.00 32.59 C ATOM 1335 CD1 PHE A 423 14.800 30.673 1.696 1.00 34.16 C ATOM 1336 CE1 PHE A 423 16.128 30.853 1.357 1.00 34.47 C ATOM 1337 CZ PHE A 423 17.056 31.142 2.336 1.00 33.24 C ATOM 1338 CE2 PHE A 423 16.654 31.246 3.647 1.00 34.02 C ATOM 1339 CD2 PHE A 423 15.342 31.079 3.977 1.00 33.39 C ATOM 1340 C PHE A 423 12.852 28.159 3.239 1.00 31.47 C ATOM 1341 O PHE A 423 13.743 27.612 2.592 1.00 31.65 O ATOM 1342 N SER A 424 12.379 27.678 4.387 1.00 30.47 N ATOM 1343 CA SER A 424 12.730 26.364 4.874 1.00 29.56 C ATOM 1344 CB SER A 424 12.038 26.069 6.182 1.00 28.62 C ATOM 1345 OG SER A 424 12.536 26.902 7.175 1.00 30.82 O ATOM 1346 C SER A 424 12.337 25.283 3.897 1.00 28.62 C ATOM 1347 O SER A 424 13.121 24.391 3.610 1.00 28.23 O ATOM 1348 N ALA A 425 11.106 25.324 3.433 1.00 28.24 N ATOM 1349 CA ALA A 425 10.643 24.333 2.465 1.00 28.61 C ATOM 1350 CB ALA A 425 9.139 24.429 2.249 1.00 28.26 C ATOM 1351 C ALA A 425 11.389 24.386 1.123 1.00 29.02 C ATOM 1352 O ALA A 425 11.530 23.372 0.434 1.00 30.06 O ATOM 1353 N PHE A 426 11.873 25.567 0.778 1.00 30.03 N ATOM 1354 CA PHE A 426 12.611 25.820 −0.451 1.00 31.03 C ATOM 1355 CB PHE A 426 12.751 27.342 −0.637 1.00 30.64 C ATOM 1356 CG PHE A 426 13.479 27.713 −1.875 1.00 33.04 C ATOM 1357 CD1 PHE A 426 12.835 27.731 −3.094 1.00 32.88 C ATOM 1358 CE1 PHE A 426 13.524 28.021 −4.238 1.00 34.86 C ATOM 1359 CZ PHE A 426 14.872 28.293 −4.189 1.00 34.01 C ATOM 1360 CE2 PHE A 426 15.515 28.287 −2.986 1.00 34.91 C ATOM 1361 CD2 PHE A 426 14.817 28.006 −1.834 1.00 35.40 C ATOM 1362 C PHE A 426 14.009 25.142 −0.447 1.00 31.56 C ATOM 1363 O PHE A 426 14.328 24.361 −1.329 1.00 31.28 O ATOM 1364 N VAL A 427 14.846 25.426 0.557 1.00 32.26 N ATOM 1365 CA VAL A 427 16.204 24.824 0.597 1.00 33.10 C ATOM 1366 CB VAL A 427 17.168 25.602 1.524 1.00 33.53 C ATOM 1367 CG1 VAL A 427 17.205 27.072 1.140 1.00 34.66 C ATOM 1368 CG2 VAL A 427 16.772 25.463 2.953 1.00 35.57 C ATOM 1369 C VAL A 427 16.186 23.370 0.987 1.00 32.54 C ATOM 1370 O VAL A 427 17.182 22.637 0.881 1.00 32.60 O ATOM 1371 N LEU A 428 15.030 22.933 1.433 1.00 33.17 N ATOM 1372 CA LEU A 428 14.895 21.543 1.788 1.00 33.15 C ATOM 1373 CB LEU A 428 13.754 21.382 2.751 1.00 33.88 C ATOM 1374 CG LEU A 428 13.731 20.007 3.346 1.00 35.63 C ATOM 1375 CD1 LEU A 428 14.751 19.913 4.473 1.00 36.29 C ATOM 1376 CD2 LEU A 428 12.345 19.712 3.830 1.00 40.57 C ATOM 1377 C LEU A 428 14.640 20.688 0.563 1.00 32.72 C ATOM 1378 O LEU A 428 15.188 19.577 0.444 1.00 32.28 O ATOM 1379 N MET A 429 13.762 21.145 −0.315 1.00 33.59 N ATOM 1380 CA MET A 429 13.441 20.428 −1.521 1.00 34.98 C ATOM 1381 CB MET A 429 11.977 20.670 −1.871 1.00 35.55 C ATOM 1382 CG MET A 429 11.036 20.479 −0.714 1.00 38.33 C ATOM 1383 SD MET A 429 10.845 18.793 −0.205 1.00 43.35 S ATOM 1384 CE MET A 429 10.460 18.095 −1.842 1.00 40.58 C ATOM 1385 C MET A 429 14.293 20.979 −2.639 1.00 35.57 C ATOM 1386 O MET A 429 13.772 21.578 −3.556 1.00 35.78 O ATOM 1387 N SER A 430 15.602 20.813 −2.559 1.00 36.04 N ATOM 1388 CA SER A 430 16.465 21.298 −3.608 1.00 37.23 C ATOM 1389 CB SER A 430 17.782 21.792 −3.060 1.00 37.79 C ATOM 1390 OG SER A 430 17.672 22.092 −1.698 1.00 40.76 O ATOM 1391 C SER A 430 16.760 20.144 −4.507 1.00 37.02 C ATOM 1392 O SER A 430 17.088 19.054 −4.034 1.00 37.47 O ATOM 1393 N ALA A 431 16.683 20.375 −5.800 1.00 37.33 N ATOM 1394 CA ALA A 431 16.869 19.301 −6.749 1.00 38.02 C ATOM 1395 CB ALA A 431 16.086 19.581 −7.999 1.00 38.37 C ATOM 1396 C ALA A 431 18.332 19.088 −7.071 1.00 39.47 C ATOM 1397 O ALA A 431 18.675 18.155 −7.801 1.00 40.70 O ATOM 1398 N ASP A 432 19.219 19.916 −6.528 1.00 40.30 N ATOM 1399 CA ASP A 432 20.619 19.731 −6.853 1.00 41.30 C ATOM 1400 CB ASP A 432 21.304 21.041 −7.201 1.00 42.25 C ATOM 1401 CG ASP A 432 21.026 22.093 −6.217 1.00 45.95 C ATOM 1402 OD1 ASP A 432 21.919 22.947 −6.001 1.00 48.76 O ATOM 1403 OD2 ASP A 432 19.930 22.144 −5.610 1.00 53.78 O ATOM 1404 C ASP A 432 21.425 18.985 −5.818 1.00 40.17 C ATOM 1405 O ASP A 432 22.623 18.843 −5.968 1.00 42.18 O ATOM 1406 N ARG A 433 20.810 18.440 −4.800 1.00 38.39 N ATOM 1407 CA ARG A 433 21.597 17.625 −3.915 1.00 37.16 C ATOM 1408 CB ARG A 433 20.744 17.081 −2.804 1.00 36.78 C ATOM 1409 CG ARG A 433 19.976 18.117 −2.084 1.00 37.06 C ATOM 1410 CD ARG A 433 20.810 19.149 −1.420 1.00 36.88 C ATOM 1411 NE ARG A 433 19.938 19.958 −0.589 1.00 38.16 N ATOM 1412 CZ ARG A 433 20.335 20.952 0.180 1.00 37.36 C ATOM 1413 NH1 ARG A 433 21.611 21.301 0.238 1.00 34.55 N ATOM 1414 NH2 ARG A 433 19.443 21.633 0.885 1.00 38.38 N ATOM 1415 C ARG A 433 22.145 16.450 −4.731 1.00 37.08 C ATOM 1416 O ARG A 433 21.441 15.925 −5.593 1.00 35.43 O ATOM 1417 N SER A 434 23.370 16.022 −4.430 1.00 36.72 N ATOM 1418 CA SER A 434 23.963 14.877 −5.105 1.00 36.76 C ATOM 1419 CB SER A 434 25.390 14.603 −4.593 1.00 36.85 C ATOM 1420 OG SER A 434 26.176 15.757 −4.604 1.00 38.46 O ATOM 1421 C SER A 434 23.196 13.630 −4.782 1.00 36.80 C ATOM 1422 O SER A 434 22.660 13.481 −3.670 1.00 35.82 O ATOM 1423 N TRP A 435 23.206 12.720 −5.754 1.00 36.33 N ATOM 1424 CA TRP A 435 22.706 11.376 −5.614 1.00 36.22 C ATOM 1425 CB TRP A 435 23.314 10.715 −4.376 1.00 36.57 C ATOM 1426 CG TRP A 435 24.778 10.979 −4.204 1.00 38.75 C ATOM 1427 CD1 TRP A 435 25.379 11.502 −3.115 1.00 40.89 C ATOM 1428 NE1 TRP A 435 26.733 11.585 −3.315 1.00 41.15 N ATOM 1429 CE2 TRP A 435 27.026 11.109 −4.560 1.00 39.69 C ATOM 1430 CD2 TRP A 435 25.825 10.717 −5.147 1.00 38.76 C ATOM 1431 CE3 TRP A 435 25.862 10.172 −6.425 1.00 40.76 C ATOM 1432 CZ3 TRP A 435 27.074 10.049 −7.063 1.00 41.43 C ATOM 1433 CH2 TRP A 435 28.250 10.450 −6.451 1.00 41.35 C ATOM 1434 CZ2 TRP A 435 28.249 10.976 −5.195 1.00 41.84 C ATOM 1435 C TRP A 435 21.193 11.264 −5.575 1.00 36.43 C ATOM 1436 O TRP A 435 20.674 10.269 −5.110 1.00 35.92 O ATOM 1437 N LEU A 436 20.483 12.272 −6.048 1.00 37.43 N ATOM 1438 CA LEU A 436 19.013 12.185 −6.139 1.00 38.64 C ATOM 1439 CB LEU A 436 18.419 13.585 −6.194 1.00 38.27 C ATOM 1440 CG LEU A 436 18.387 14.376 −4.902 1.00 37.94 C ATOM 1441 CD1 LEU A 436 17.844 15.752 −5.190 1.00 38.90 C ATOM 1442 CD2 LEU A 436 17.547 13.667 −3.885 1.00 37.76 C ATOM 1443 C LEU A 436 18.531 11.436 −7.394 1.00 40.22 C ATOM 1444 O LEU A 436 19.022 11.691 −8.497 1.00 40.43 O ATOM 1445 N GLN A 437 17.542 10.562 −7.241 1.00 42.27 N ATOM 1446 CA GLN A 437 16.981 9.825 −8.370 1.00 43.95 C ATOM 1447 CB GLN A 437 16.334 8.537 −7.896 1.00 44.38 C ATOM 1448 CG GLN A 437 17.247 7.710 −7.059 1.00 46.96 C ATOM 1449 CD GLN A 437 16.647 6.389 −6.653 1.00 50.03 C ATOM 1450 OE1 GLN A 437 15.546 6.043 −7.084 1.00 54.83 O ATOM 1451 NE2 GLN A 437 17.370 5.640 −5.826 1.00 50.03 N ATOM 1452 C GLN A 437 15.958 10.644 −9.136 1.00 44.68 C ATOM 1453 O GLN A 437 16.051 10.788 −10.346 1.00 45.04 O ATOM 1454 N GLU A 438 15.000 11.221 −8.433 1.00 45.84 N ATOM 1455 CA GLU A 438 13.933 11.977 −9.093 1.00 46.74 C ATOM 1456 CB GLU A 438 12.628 11.716 −8.360 1.00 47.49 C ATOM 1457 CG GLU A 438 12.433 10.254 −8.005 1.00 49.80 C ATOM 1458 CD GLU A 438 11.318 10.066 −7.011 1.00 54.24 C ATOM 1459 OE1 GLU A 438 10.145 10.256 −7.410 1.00 55.09 O ATOM 1460 OE2 GLU A 438 11.625 9.744 −5.832 1.00 58.98 O ATOM 1461 C GLU A 438 14.169 13.475 −9.154 1.00 46.63 C ATOM 1462 O GLU A 438 13.399 14.242 −8.586 1.00 47.40 O ATOM 1463 N LYS A 439 15.192 13.897 −9.887 1.00 46.50 N ATOM 1464 CA LYS A 439 15.535 15.311 −9.995 1.00 45.87 C ATOM 1465 CB LYS A 439 16.834 15.521 −10.794 1.00 46.05 C ATOM 1466 CG LYS A 439 18.096 14.931 −10.113 1.00 48.48 C ATOM 1467 CD LYS A 439 19.417 15.775 −10.247 1.00 51.35 C ATOM 1468 CE LYS A 439 20.205 15.702 −8.875 1.00 54.04 C ATOM 1469 NZ LYS A 439 21.624 16.236 −8.775 1.00 53.95 N ATOM 1470 C LYS A 439 14.405 16.129 −10.609 1.00 45.17 C ATOM 1471 O LYS A 439 14.149 17.248 −10.179 1.00 44.73 O ATOM 1472 N VAL A 440 13.723 15.582 −11.607 1.00 44.46 N ATOM 1473 CA VAL A 440 12.665 16.324 −12.279 1.00 43.79 C ATOM 1474 CB VAL A 440 12.234 15.633 −13.601 1.00 44.85 C ATOM 1475 CG1 VAL A 440 10.895 16.199 −14.096 1.00 43.93 C ATOM 1476 CG2 VAL A 440 13.359 15.762 −14.686 1.00 44.89 C ATOM 1477 C VAL A 440 11.437 16.574 −11.385 1.00 42.76 C ATOM 1478 O VAL A 440 10.908 17.667 −11.371 1.00 42.48 O ATOM 1479 N LYS A 441 10.981 15.582 −10.638 1.00 42.10 N ATOM 1480 CA LYS A 441 9.842 15.811 −9.737 1.00 42.12 C ATOM 1481 CB LYS A 441 9.337 14.469 −9.167 1.00 42.37 C ATOM 1482 CG LYS A 441 8.268 14.551 −8.058 1.00 44.18 C ATOM 1483 CD LYS A 441 7.770 13.145 −7.635 1.00 46.69 C ATOM 1484 CE LYS A 441 7.415 13.029 −6.135 1.00 48.06 C ATOM 1485 NZ LYS A 441 6.374 13.988 −5.640 1.00 50.40 N ATOM 1486 C LYS A 441 10.222 16.812 −8.621 1.00 41.30 C ATOM 1487 O LYS A 441 9.493 17.751 −8.337 1.00 41.41 O ATOM 1488 N ILE A 442 11.384 16.639 −8.016 1.00 40.14 N ATOM 1489 CA ILE A 442 11.792 17.530 −6.947 1.00 39.47 C ATOM 1490 CB ILE A 442 13.092 17.036 −6.347 1.00 39.22 C ATOM 1491 CG1 ILE A 442 12.817 15.709 −5.642 1.00 37.84 C ATOM 1492 CD1 ILE A 442 14.038 14.971 −5.155 1.00 36.84 C ATOM 1493 CG2 ILE A 442 13.694 18.109 −5.421 1.00 38.41 C ATOM 1494 C ILE A 442 11.924 18.939 −7.475 1.00 40.04 C ATOM 1495 O ILE A 442 11.519 19.907 −6.828 1.00 39.89 O ATOM 1496 N GLU A 443 12.474 19.068 −8.671 1.00 40.56 N ATOM 1497 CA GLU A 443 12.583 20.380 −9.305 1.00 41.62 C ATOM 1498 CB GLU A 443 13.325 20.252 −10.625 1.00 42.43 C ATOM 1499 CG GLU A 443 13.473 21.556 −11.384 1.00 46.01 C ATOM 1500 CD GLU A 443 14.586 22.409 −10.832 1.00 52.43 C ATOM 1501 OE1 GLU A 443 15.520 21.840 −10.224 1.00 58.50 O ATOM 1502 OE2 GLU A 443 14.540 23.649 −10.991 1.00 56.77 O ATOM 1503 C GLU A 443 11.221 21.041 −9.531 1.00 41.19 C ATOM 1504 O GLU A 443 11.051 22.217 −9.257 1.00 41.75 O ATOM 1505 N LYS A 444 10.241 20.309 −10.027 1.00 41.34 N ATOM 1506 CA LYS A 444 8.918 20.906 −10.222 1.00 41.91 C ATOM 1507 CB LYS A 444 7.954 19.921 −10.887 1.00 42.50 C ATOM 1508 CG LYS A 444 8.359 19.402 −12.287 1.00 46.11 C ATOM 1509 CD LYS A 444 8.622 20.539 −13.249 1.00 50.76 C ATOM 1510 CE LYS A 444 9.166 20.064 −14.593 1.00 53.57 C ATOM 1511 NZ LYS A 444 10.041 21.141 −15.193 1.00 55.91 N ATOM 1512 C LYS A 444 8.333 21.367 −8.869 1.00 41.11 C ATOM 1513 O LYS A 444 7.669 22.385 −8.787 1.00 40.91 O ATOM 1514 N LEU A 445 8.564 20.599 −7.811 1.00 40.57 N ATOM 1515 CA LEU A 445 8.100 20.993 −6.475 1.00 40.29 C ATOM 1516 CB LEU A 445 8.291 19.823 −5.510 1.00 40.73 C ATOM 1517 CG LEU A 445 7.471 18.577 −5.846 1.00 43.76 C ATOM 1518 CD1 LEU A 445 8.070 17.339 −5.224 1.00 46.83 C ATOM 1519 CD2 LEU A 445 6.006 18.699 −5.405 1.00 45.67 C ATOM 1520 C LEU A 445 8.802 22.264 −5.932 1.00 39.05 C ATOM 1521 O LEU A 445 8.162 23.148 −5.355 1.00 38.44 O ATOM 1522 N GLN A 446 10.113 22.379 −6.131 1.00 37.84 N ATOM 1523 CA GLN A 446 10.804 23.553 −5.630 1.00 37.19 C ATOM 1524 CB GLN A 446 12.322 23.443 −5.770 1.00 36.98 C ATOM 1525 CG GLN A 446 13.058 24.617 −5.128 1.00 38.75 C ATOM 1526 CD GLN A 446 14.563 24.588 −5.312 1.00 40.58 C ATOM 1527 OE1 GLN A 446 15.065 24.583 −6.428 1.00 42.73 O ATOM 1528 NE2 GLN A 446 15.284 24.599 −4.206 1.00 41.51 N ATOM 1529 C GLN A 446 10.312 24.808 −6.332 1.00 36.39 C ATOM 1530 O GLN A 446 10.218 25.880 −5.715 1.00 35.15 O ATOM 1531 N GLN A 447 10.037 24.680 −7.626 1.00 36.58 N ATOM 1532 CA GLN A 447 9.547 25.810 −8.415 1.00 37.09 C ATOM 1533 CB GLN A 447 9.316 25.428 −9.872 1.00 37.88 C ATOM 1534 CG GLN A 447 10.545 25.058 −10.659 1.00 42.37 C ATOM 1535 CD GLN A 447 10.176 24.683 −12.104 1.00 49.26 C ATOM 1536 OE1 GLN A 447 9.144 25.147 −12.634 1.00 53.32 O ATOM 1537 NE2 GLN A 447 10.993 23.831 −12.729 1.00 52.11 N ATOM 1538 C GLN A 447 8.231 26.343 −7.845 1.00 35.60 C ATOM 1539 O GLN A 447 8.075 27.518 −7.726 1.00 33.62 O ATOM 1540 N LYS A 448 7.305 25.461 −7.508 1.00 35.56 N ATOM 1541 CA LYS A 448 6.055 25.897 −6.903 1.00 36.26 C ATOM 1542 CB LYS A 448 5.125 24.707 −6.684 1.00 36.75 C ATOM 1543 CG LYS A 448 4.434 24.265 −7.968 1.00 41.05 C ATOM 1544 CD LYS A 448 3.642 22.962 −7.752 1.00 45.62 C ATOM 1545 CE LYS A 448 2.734 22.623 −8.941 1.00 47.75 C ATOM 1546 NZ LYS A 448 1.655 21.655 −8.507 1.00 51.38 N ATOM 1547 C LYS A 448 6.304 26.615 −5.584 1.00 35.43 C ATOM 1548 O LYS A 448 5.762 27.697 −5.345 1.00 34.04 O ATOM 1549 N ILE A 449 7.118 25.997 −4.720 1.00 35.23 N ATOM 1550 CA ILE A 449 7.422 26.574 −3.428 1.00 35.08 C ATOM 1551 CB ILE A 449 8.400 25.663 −2.647 1.00 35.31 C ATOM 1552 CG1 ILE A 449 7.662 24.412 −2.135 1.00 34.62 C ATOM 1553 CD1 ILE A 449 8.565 23.272 −1.666 1.00 35.68 C ATOM 1554 CG2 ILE A 449 9.036 26.439 −1.508 1.00 34.70 C ATOM 1555 C ILE A 449 8.009 27.950 −3.648 1.00 35.67 C ATOM 1556 O ILE A 449 7.663 28.891 −2.954 1.00 36.39 O ATOM 1557 N GLN A 450 8.863 28.092 −4.648 1.00 36.15 N ATOM 1558 CA GLN A 450 9.491 29.383 −4.898 1.00 37.22 C ATOM 1559 CB GLN A 450 10.624 29.245 −5.929 1.00 37.71 C ATOM 1560 CG GLN A 450 11.440 30.525 −6.143 1.00 39.93 C ATOM 1561 CD GLN A 450 12.459 30.381 −7.271 1.00 44.24 C ATOM 1562 OE1 GLN A 450 13.107 29.339 −7.409 1.00 46.56 O ATOM 1563 NE2 GLN A 450 12.603 31.421 −8.071 1.00 46.99 N ATOM 1564 C GLN A 450 8.497 30.453 −5.351 1.00 37.23 C ATOM 1565 O GLN A 450 8.668 31.629 −5.033 1.00 36.57 O ATOM 1566 N LEU A 451 7.460 30.067 −6.095 1.00 37.47 N ATOM 1567 CA LEU A 451 6.491 31.055 −6.548 1.00 38.17 C ATOM 1568 CB LEU A 451 5.602 30.496 −7.658 1.00 39.23 C ATOM 1569 CG LEU A 451 6.299 30.228 −8.992 1.00 40.16 C ATOM 1570 CD1 LEU A 451 5.417 29.356 −9.874 1.00 42.60 C ATOM 1571 CD2 LEU A 451 6.671 31.543 −9.709 1.00 40.87 C ATOM 1572 C LEU A 451 5.675 31.479 −5.350 1.00 38.38 C ATOM 1573 O LEU A 451 5.328 32.670 −5.177 1.00 37.56 O ATOM 1574 N ALA A 452 5.396 30.500 −4.499 1.00 38.51 N ATOM 1575 CA ALA A 452 4.683 30.763 −3.261 1.00 39.16 C ATOM 1576 CB ALA A 452 4.352 29.452 −2.566 1.00 39.25 C ATOM 1577 C ALA A 452 5.492 31.668 −2.335 1.00 39.16 C ATOM 1578 O ALA A 452 4.960 32.541 −1.667 1.00 38.45 O ATOM 1579 N LEU A 453 6.793 31.461 −2.302 1.00 39.99 N ATOM 1580 CA LEU A 453 7.650 32.284 −1.454 1.00 40.16 C ATOM 1581 CB LEU A 453 9.078 31.735 −1.455 1.00 39.61 C ATOM 1582 CG LEU A 453 10.108 32.594 −0.724 1.00 38.75 C ATOM 1583 CD1 LEU A 453 9.785 32.702 0.737 1.00 37.68 C ATOM 1584 CD2 LEU A 453 11.487 31.994 −0.924 1.00 39.28 C ATOM 1585 C LEU A 453 7.649 33.727 −1.936 1.00 41.01 C ATOM 1586 O LEU A 453 7.559 34.652 −1.143 1.00 40.74 O ATOM 1587 N GLN A 454 7.784 33.912 −3.245 1.00 43.21 N ATOM 1588 CA GLN A 454 7.778 35.242 −3.857 1.00 44.37 C ATOM 1589 CB GLN A 454 8.018 35.097 −5.353 1.00 44.93 C ATOM 1590 CG GLN A 454 8.139 36.413 −6.092 1.00 47.00 C ATOM 1591 CD GLN A 454 8.484 36.232 −7.549 1.00 50.13 C ATOM 1592 OE1 GLN A 454 7.937 35.355 −8.224 1.00 51.04 O ATOM 1593 NE2 GLN A 454 9.397 37.062 −8.044 1.00 52.53 N ATOM 1594 C GLN A 454 6.438 35.937 −3.580 1.00 45.15 C ATOM 1595 O GLN A 454 6.385 37.105 −3.193 1.00 45.17 O ATOM 1596 N HIS A 455 5.363 35.186 −3.735 1.00 46.23 N ATOM 1597 CA HIS A 455 4.029 35.654 −3.418 1.00 47.70 C ATOM 1598 CB HIS A 455 3.064 34.479 −3.557 1.00 47.88 C ATOM 1599 CG HIS A 455 1.659 34.782 −3.164 1.00 50.63 C ATOM 1600 ND1 HIS A 455 0.939 35.826 −3.706 1.00 52.70 N ATOM 1601 CE1 HIS A 455 −0.272 35.843 −3.172 1.00 53.57 C ATOM 1602 NE2 HIS A 455 −0.363 34.844 −2.309 1.00 53.78 N ATOM 1603 CD2 HIS A 455 0.833 34.167 −2.283 1.00 52.74 C ATOM 1604 C HIS A 455 3.974 36.276 −2.018 1.00 48.21 C ATOM 1605 O HIS A 455 3.561 37.425 −1.852 1.00 48.61 O ATOM 1606 N VAL A 456 4.436 35.544 −1.017 1.00 48.96 N ATOM 1607 CA VAL A 456 4.409 36.035 0.369 1.00 49.83 C ATOM 1608 CB VAL A 456 4.656 34.884 1.353 1.00 49.91 C ATOM 1609 CG1 VAL A 456 4.882 35.394 2.759 1.00 50.35 C ATOM 1610 CG2 VAL A 456 3.498 33.899 1.325 1.00 50.07 C ATOM 1611 C VAL A 456 5.437 37.101 0.684 1.00 50.39 C ATOM 1612 O VAL A 456 5.262 37.865 1.625 1.00 50.47 O ATOM 1613 N LEU A 457 6.529 37.119 −0.062 1.00 51.74 N ATOM 1614 CA LEU A 457 7.538 38.140 0.143 1.00 53.31 C ATOM 1615 CB LEU A 457 8.801 37.829 −0.648 1.00 53.04 C ATOM 1616 CG LEU A 457 9.664 36.711 −0.065 1.00 52.30 C ATOM 1617 CD1 LEU A 457 10.705 36.350 −1.081 1.00 51.56 C ATOM 1618 CD2 LEU A 457 10.296 37.172 1.254 1.00 50.93 C ATOM 1619 C LEU A 457 6.979 39.480 −0.294 1.00 55.43 C ATOM 1620 O LEU A 457 7.071 40.456 0.437 1.00 54.68 O ATOM 1621 N GLN A 458 6.372 39.516 −1.480 1.00 58.58 N ATOM 1622 CA GLN A 458 5.836 40.764 −2.020 1.00 61.31 C ATOM 1623 CB GLN A 458 5.596 40.661 −3.538 1.00 61.66 C ATOM 1624 CG GLN A 458 4.556 39.646 −4.008 1.00 63.40 C ATOM 1625 CD GLN A 458 4.816 39.189 −5.449 1.00 65.86 C ATOM 1626 OE1 GLN A 458 5.793 39.622 −6.069 1.00 67.19 O ATOM 1627 NE2 GLN A 458 3.949 38.313 −5.978 1.00 66.76 N ATOM 1628 C GLN A 458 4.591 41.256 −1.265 1.00 63.26 C ATOM 1629 O GLN A 458 4.268 42.434 −1.282 1.00 63.33 O ATOM 1630 N LYS A 459 3.929 40.359 −0.560 1.00 65.71 N ATOM 1631 CA LYS A 459 2.770 40.732 0.228 1.00 67.66 C ATOM 1632 CB LYS A 459 2.241 39.477 0.894 1.00 67.68 C ATOM 1633 CG LYS A 459 1.061 39.617 1.825 1.00 67.62 C ATOM 1634 CD LYS A 459 0.638 38.243 2.332 1.00 67.67 C ATOM 1635 CE LYS A 459 −0.042 37.427 1.241 1.00 67.92 C ATOM 1636 NZ LYS A 459 −0.160 35.983 1.597 1.00 68.58 N ATOM 1637 C LYS A 459 3.116 41.776 1.290 1.00 69.97 C ATOM 1638 O LYS A 459 2.285 42.618 1.648 1.00 70.29 O ATOM 1639 N ASN A 460 4.361 41.747 1.755 1.00 72.42 N ATOM 1640 CA ASN A 460 4.802 42.571 2.871 1.00 74.25 C ATOM 1641 CB ASN A 460 5.508 41.681 3.896 1.00 74.44 C ATOM 1642 CG ASN A 460 4.624 40.534 4.390 1.00 74.77 C ATOM 1643 OD1 ASN A 460 3.556 40.762 4.964 1.00 74.61 O ATOM 1644 ND2 ASN A 460 5.071 39.292 4.165 1.00 74.61 N ATOM 1645 C ASN A 460 5.731 43.721 2.501 1.00 76.15 C ATOM 1646 O ASN A 460 5.676 44.785 3.123 1.00 76.33 O ATOM 1647 N HIS A 461 6.582 43.529 1.496 1.00 78.30 N ATOM 1648 CA HIS A 461 7.564 44.550 1.141 1.00 79.89 C ATOM 1649 CB HIS A 461 8.846 44.307 1.932 1.00 80.20 C ATOM 1650 CG HIS A 461 8.629 44.208 3.407 1.00 81.84 C ATOM 1651 ND1 HIS A 461 8.597 45.312 4.234 1.00 84.02 N ATOM 1652 CE1 HIS A 461 8.377 44.919 5.478 1.00 84.23 C ATOM 1653 NE2 HIS A 461 8.253 43.603 5.484 1.00 83.90 N ATOM 1654 CD2 HIS A 461 8.406 43.135 4.201 1.00 83.33 C ATOM 1655 C HIS A 461 7.907 44.600 −0.344 1.00 80.88 C ATOM 1656 O HIS A 461 9.067 44.431 −0.721 1.00 80.77 O ATOM 1657 N ARG A 462 6.912 44.841 −1.191 1.00 82.27 N ATOM 1658 CA ARG A 462 7.194 45.051 −2.605 1.00 83.28 C ATOM 1659 CB ARG A 462 5.903 45.330 −3.393 1.00 83.78 C ATOM 1660 CG ARG A 462 5.303 44.070 −4.042 1.00 85.00 C ATOM 1661 CD ARG A 462 3.898 44.230 −4.665 1.00 86.49 C ATOM 1662 NE ARG A 462 3.505 43.033 −5.417 1.00 87.52 N ATOM 1663 CZ ARG A 462 2.281 42.778 −5.865 1.00 88.16 C ATOM 1664 NH1 ARG A 462 1.283 43.636 −5.655 1.00 88.54 N ATOM 1665 NH2 ARG A 462 2.056 41.653 −6.532 1.00 87.86 N ATOM 1666 C ARG A 462 8.191 46.222 −2.687 1.00 83.63 C ATOM 1667 O ARG A 462 8.541 46.699 −3.770 1.00 83.73 O ATOM 1668 N GLU A 463 8.649 46.649 −1.506 1.00 83.89 N ATOM 1669 CA GLU A 463 9.624 47.723 −1.335 1.00 83.96 C ATOM 1670 CB GLU A 463 9.847 47.970 0.156 1.00 84.16 C ATOM 1671 CG GLU A 463 10.746 46.939 0.821 1.00 84.97 C ATOM 1672 CD GLU A 463 10.741 47.071 2.326 1.00 85.96 C ATOM 1673 OE1 GLU A 463 10.286 48.126 2.808 1.00 87.00 O ATOM 1674 OE2 GLU A 463 11.182 46.126 3.020 1.00 86.69 O ATOM 1675 C GLU A 463 10.980 47.413 −1.965 1.00 83.47 C ATOM 1676 O GLU A 463 11.752 48.325 −2.276 1.00 83.54 O ATOM 1677 N ASP A 464 11.274 46.125 −2.115 1.00 82.69 N ATOM 1678 CA ASP A 464 12.532 45.673 −2.691 1.00 82.00 C ATOM 1679 CB ASP A 464 13.576 45.440 −1.582 1.00 82.03 C ATOM 1680 CG ASP A 464 14.138 46.743 −1.000 1.00 82.58 C ATOM 1681 OD1 ASP A 464 13.981 47.814 −1.626 1.00 82.80 O ATOM 1682 OD2 ASP A 464 14.766 46.795 0.079 1.00 82.96 O ATOM 1683 C ASP A 464 12.251 44.380 −3.467 1.00 81.10 C ATOM 1684 O ASP A 464 11.103 44.121 −3.868 1.00 81.10 O ATOM 1685 N GLY A 465 13.305 43.599 −3.701 1.00 79.69 N ATOM 1686 CA GLY A 465 13.210 42.292 −4.339 1.00 78.42 C ATOM 1687 C GLY A 465 14.125 41.358 −3.567 1.00 77.09 C ATOM 1688 O GLY A 465 15.055 40.776 −4.128 1.00 76.83 O ATOM 1689 N ILE A 466 13.839 41.229 −2.269 1.00 75.34 N ATOM 1690 CA ILE A 466 14.687 40.507 −1.318 1.00 73.67 C ATOM 1691 CB ILE A 466 14.195 40.728 0.123 1.00 73.83 C ATOM 1692 CG1 ILE A 466 13.734 42.163 0.325 1.00 74.49 C ATOM 1693 CD1 ILE A 466 13.216 42.442 1.714 1.00 75.46 C ATOM 1694 CG2 ILE A 466 15.312 40.453 1.110 1.00 74.24 C ATOM 1695 C ILE A 466 14.756 39.023 −1.579 1.00 71.72 C ATOM 1696 O ILE A 466 15.601 38.329 −1.009 1.00 71.07 O ATOM 1697 N LEU A 467 13.860 38.535 −2.425 1.00 69.76 N ATOM 1698 CA LEU A 467 13.872 37.134 −2.791 1.00 68.62 C ATOM 1699 CB LEU A 467 12.849 36.853 −3.889 1.00 68.53 C ATOM 1700 CG LEU A 467 12.722 35.400 −4.353 1.00 68.87 C ATOM 1701 CD1 LEU A 467 12.138 34.497 −3.294 1.00 69.10 C ATOM 1702 CD2 LEU A 467 11.854 35.347 −5.579 1.00 70.26 C ATOM 1703 C LEU A 467 15.273 36.746 −3.247 1.00 67.31 C ATOM 1704 O LEU A 467 15.733 35.642 −2.961 1.00 67.18 O ATOM 1705 N THR A 468 15.954 37.660 −3.934 1.00 65.58 N ATOM 1706 CA THR A 468 17.285 37.382 −4.452 1.00 64.62 C ATOM 1707 CB THR A 468 17.695 38.399 −5.584 1.00 64.88 C ATOM 1708 OG1 THR A 468 17.784 39.733 −5.065 1.00 64.25 O ATOM 1709 CG2 THR A 468 16.631 38.493 −6.680 1.00 64.06 C ATOM 1710 C THR A 468 18.316 37.367 −3.331 1.00 63.63 C ATOM 1711 O THR A 468 19.200 36.515 −3.298 1.00 63.53 O ATOM 1712 N LYS A 469 18.215 38.324 −2.420 1.00 62.39 N ATOM 1713 CA LYS A 469 19.088 38.367 −1.252 1.00 61.38 C ATOM 1714 CB LYS A 469 18.797 39.647 −0.484 1.00 62.13 C ATOM 1715 CG LYS A 469 19.486 39.829 0.860 1.00 62.89 C ATOM 1716 CD LYS A 469 19.256 41.310 1.276 1.00 64.52 C ATOM 1717 CE LYS A 469 19.505 41.608 2.756 1.00 65.74 C ATOM 1718 NZ LYS A 469 18.942 42.951 3.178 1.00 66.28 N ATOM 1719 C LYS A 469 18.854 37.133 −0.355 1.00 59.69 C ATOM 1720 O LYS A 469 19.766 36.645 0.317 1.00 59.53 O ATOM 1721 N LEU A 470 17.627 36.633 −0.360 1.00 57.33 N ATOM 1722 CA LEU A 470 17.292 35.439 0.387 1.00 56.01 C ATOM 1723 CB LEU A 470 15.771 35.324 0.527 1.00 55.44 C ATOM 1724 CG LEU A 470 15.242 34.622 1.770 1.00 54.97 C ATOM 1725 CD1 LEU A 470 15.881 35.167 3.018 1.00 54.08 C ATOM 1726 CD2 LEU A 470 13.721 34.701 1.859 1.00 56.05 C ATOM 1727 C LEU A 470 17.861 34.213 −0.331 1.00 55.43 C ATOM 1728 O LEU A 470 18.522 33.382 0.281 1.00 54.90 O ATOM 1729 N ILE A 471 17.624 34.111 −1.635 1.00 54.68 N ATOM 1730 CA ILE A 471 18.120 32.986 −2.412 1.00 54.43 C ATOM 1731 CB ILE A 471 17.538 33.016 −3.836 1.00 54.76 C ATOM 1732 CG1 ILE A 471 16.097 32.526 −3.792 1.00 55.40 C ATOM 1733 CD1 ILE A 471 15.438 32.478 −5.119 1.00 56.34 C ATOM 1734 CG2 ILE A 471 18.372 32.144 −4.798 1.00 55.26 C ATOM 1735 C ILE A 471 19.631 33.016 −2.433 1.00 53.73 C ATOM 1736 O ILE A 471 20.281 31.996 −2.616 1.00 53.69 O ATOM 1737 N CYS A 472 20.189 34.198 −2.239 1.00 52.86 N ATOM 1738 CA CYS A 472 21.625 34.347 −2.120 1.00 52.63 C ATOM 1739 CB CYS A 472 21.979 35.829 −1.990 1.00 52.92 C ATOM 1740 SG CYS A 472 22.874 36.495 −3.399 1.00 58.34 S ATOM 1741 C CYS A 472 22.157 33.604 −0.886 1.00 50.97 C ATOM 1742 O CYS A 472 23.290 33.104 −0.901 1.00 50.65 O ATOM 1743 N LYS A 473 21.348 33.555 0.179 1.00 48.54 N ATOM 1744 CA LYS A 473 21.758 32.936 1.439 1.00 47.29 C ATOM 1745 CB LYS A 473 20.754 33.227 2.562 1.00 47.39 C ATOM 1746 CG LYS A 473 20.619 34.712 2.930 1.00 49.59 C ATOM 1747 CD LYS A 473 21.832 35.243 3.708 1.00 52.10 C ATOM 1748 CE LYS A 473 22.062 36.733 3.414 1.00 54.59 C ATOM 1749 NZ LYS A 473 23.470 37.017 2.981 1.00 56.43 N ATOM 1750 C LYS A 473 21.875 31.450 1.277 1.00 45.26 C ATOM 1751 O LYS A 473 22.631 30.804 1.995 1.00 45.05 O ATOM 1752 N VAL A 474 21.122 30.919 0.327 1.00 43.23 N ATOM 1753 CA VAL A 474 21.136 29.518 0.102 1.00 42.19 C ATOM 1754 CB VAL A 474 20.387 29.116 −1.145 1.00 42.59 C ATOM 1755 CG1 VAL A 474 20.645 27.663 −1.449 1.00 42.42 C ATOM 1756 CG2 VAL A 474 18.910 29.383 −0.957 1.00 42.39 C ATOM 1757 C VAL A 474 22.546 29.055 −0.055 1.00 41.04 C ATOM 1758 O VAL A 474 22.919 28.042 0.503 1.00 39.72 O ATOM 1759 N SER A 475 23.345 29.780 −0.812 1.00 39.27 N ATOM 1760 CA SER A 475 24.718 29.353 −0.979 1.00 38.63 C ATOM 1761 CB SER A 475 25.402 30.157 −2.070 1.00 38.92 C ATOM 1762 OG SER A 475 26.788 29.921 −2.029 1.00 40.43 O ATOM 1763 C SER A 475 25.490 29.483 0.336 1.00 37.50 C ATOM 1764 O SER A 475 26.430 28.759 0.576 1.00 36.17 O ATOM 1765 N THR A 476 25.118 30.425 1.192 1.00 36.92 N ATOM 1766 CA THR A 476 25.854 30.597 2.443 1.00 36.78 C ATOM 1767 CB THR A 476 25.460 31.898 3.133 1.00 37.27 C ATOM 1768 OG1 THR A 476 25.293 32.946 2.166 1.00 39.90 O ATOM 1769 CG2 THR A 476 26.543 32.416 4.043 1.00 37.41 C ATOM 1770 C THR A 476 25.588 29.423 3.378 1.00 36.02 C ATOM 1771 O THR A 476 26.489 28.981 4.084 1.00 35.49 O ATOM 1772 N LEU A 477 24.355 28.916 3.360 1.00 35.62 N ATOM 1773 CA LEU A 477 23.939 27.801 4.200 1.00 35.50 C ATOM 1774 CB LEU A 477 22.457 27.515 4.019 1.00 35.72 C ATOM 1775 CG LEU A 477 21.480 28.292 4.875 1.00 35.56 C ATOM 1776 CD1 LEU A 477 20.057 28.141 4.321 1.00 36.36 C ATOM 1777 CD2 LEU A 477 21.584 27.800 6.279 1.00 33.36 C ATOM 1778 C LEU A 477 24.670 26.538 3.890 1.00 35.75 C ATOM 1779 O LEU A 477 24.966 25.754 4.792 1.00 35.71 O ATOM 1780 N ARG A 478 24.941 26.311 2.610 1.00 35.96 N ATOM 1781 CA ARG A 478 25.659 25.124 2.183 1.00 36.68 C ATOM 1782 CB ARG A 478 25.606 24.989 0.666 1.00 37.49 C ATOM 1783 CG ARG A 478 24.216 24.645 0.185 1.00 39.62 C ATOM 1784 CD ARG A 478 24.110 24.375 −1.293 1.00 41.13 C ATOM 1785 NE ARG A 478 22.727 24.112 −1.658 1.00 42.25 N ATOM 1786 CZ ARG A 478 22.342 23.503 −2.763 1.00 43.78 C ATOM 1787 NH1 ARG A 478 23.246 23.088 −3.641 1.00 45.06 N ATOM 1788 NH2 ARG A 478 21.045 23.312 −3.003 1.00 42.39 N ATOM 1789 C ARG A 478 27.093 25.179 2.666 1.00 36.22 C ATOM 1790 O ARG A 478 27.655 24.170 3.056 1.00 36.31 O ATOM 1791 N ALA A 479 27.690 26.361 2.645 1.00 35.43 N ATOM 1792 CA ALA A 479 29.045 26.502 3.144 1.00 34.83 C ATOM 1793 CB ALA A 479 29.634 27.829 2.714 1.00 34.35 C ATOM 1794 C ALA A 479 29.029 26.382 4.674 1.00 34.50 C ATOM 1795 O ALA A 479 29.923 25.803 5.254 1.00 33.03 O ATOM 1796 N LEU A 480 28.011 26.924 5.330 1.00 34.39 N ATOM 1797 CA LEU A 480 27.931 26.756 6.768 1.00 35.19 C ATOM 1798 CB LEU A 480 26.787 27.598 7.348 1.00 35.91 C ATOM 1799 CG LEU A 480 26.747 27.805 8.845 1.00 35.84 C ATOM 1800 CD1 LEU A 480 28.051 28.355 9.382 1.00 37.04 C ATOM 1801 CD2 LEU A 480 25.590 28.734 9.189 1.00 36.87 C ATOM 1802 C LEU A 480 27.787 25.276 7.138 1.00 35.48 C ATOM 1803 O LEU A 480 28.525 24.768 7.999 1.00 36.43 O ATOM 1804 N CYS A 481 26.886 24.557 6.482 1.00 34.90 N ATOM 1805 CA CYS A 481 26.721 23.150 6.768 1.00 35.75 C ATOM 1806 CB CYS A 481 25.408 22.617 6.151 1.00 35.51 C ATOM 1807 SG CYS A 481 23.970 23.492 6.880 1.00 39.57 S ATOM 1808 C CYS A 481 27.955 22.339 6.343 1.00 35.95 C ATOM 1809 O CYS A 481 28.248 21.278 6.914 1.00 35.58 O ATOM 1810 N GLY A 482 28.690 22.846 5.359 1.00 35.86 N ATOM 1811 CA GLY A 482 29.909 22.197 4.922 1.00 35.86 C ATOM 1812 C GLY A 482 30.978 22.309 5.983 1.00 35.56 C ATOM 1813 O GLY A 482 31.689 21.375 6.268 1.00 35.07 O ATOM 1814 N ARG A 483 31.111 23.464 6.587 1.00 36.33 N ATOM 1815 CA ARG A 483 32.099 23.572 7.623 1.00 37.63 C ATOM 1816 CB ARG A 483 32.250 25.000 8.046 1.00 38.73 C ATOM 1817 CG ARG A 483 32.770 25.873 6.900 1.00 43.48 C ATOM 1818 CD ARG A 483 34.089 26.567 7.220 1.00 48.75 C ATOM 1819 NE ARG A 483 34.129 27.928 6.699 1.00 52.27 N ATOM 1820 CZ ARG A 483 34.148 29.016 7.463 1.00 56.41 C ATOM 1821 NH1 ARG A 483 34.138 28.914 8.793 1.00 55.60 N ATOM 1822 NH2 ARG A 483 34.177 30.224 6.894 1.00 59.68 N ATOM 1823 C ARG A 483 31.767 22.661 8.813 1.00 37.14 C ATOM 1824 O ARG A 483 32.662 22.026 9.401 1.00 36.58 O ATOM 1825 N HIS A 484 30.486 22.567 9.161 1.00 36.27 N ATOM 1826 CA HIS A 484 30.119 21.712 10.270 1.00 35.26 C ATOM 1827 CB HIS A 484 28.615 21.655 10.449 1.00 34.25 C ATOM 1828 CG HIS A 484 28.161 20.599 11.394 1.00 31.44 C ATOM 1829 ND1 HIS A 484 27.481 19.481 10.975 1.00 26.89 N ATOM 1830 CE1 HIS A 484 27.178 18.740 12.032 1.00 29.68 C ATOM 1831 NE2 HIS A 484 27.689 19.307 13.111 1.00 26.36 N ATOM 1832 CD2 HIS A 484 28.293 20.484 12.740 1.00 29.62 C ATOM 1833 C HIS A 484 30.656 20.333 10.013 1.00 36.35 C ATOM 1834 O HIS A 484 31.264 19.740 10.893 1.00 35.93 O ATOM 1835 N THR A 485 30.457 19.818 8.805 1.00 38.13 N ATOM 1836 CA THR A 485 30.881 18.466 8.520 1.00 39.75 C ATOM 1837 CB THR A 485 30.421 18.032 7.111 1.00 40.58 C ATOM 1838 OG1 THR A 485 29.011 17.726 7.102 1.00 42.13 O ATOM 1839 CG2 THR A 485 31.050 16.685 6.702 1.00 41.01 C ATOM 1840 C THR A 485 32.404 18.340 8.663 1.00 40.64 C ATOM 1841 O THR A 485 32.903 17.312 9.092 1.00 41.11 O ATOM 1842 N GLU A 486 33.136 19.380 8.297 1.00 41.10 N ATOM 1843 CA GLU A 486 34.583 19.329 8.343 1.00 41.77 C ATOM 1844 CB GLU A 486 35.200 20.533 7.597 1.00 42.58 C ATOM 1845 CG GLU A 486 35.297 20.311 6.080 1.00 45.90 C ATOM 1846 CD GLU A 486 35.265 21.577 5.215 1.00 48.00 C ATOM 1847 OE1 GLU A 486 34.972 21.411 4.013 1.00 50.12 O ATOM 1848 OE2 GLU A 486 35.538 22.715 5.690 1.00 50.93 O ATOM 1849 C GLU A 486 35.048 19.311 9.775 1.00 40.94 C ATOM 1850 O GLU A 486 35.970 18.573 10.146 1.00 40.53 O ATOM 1851 N LYS A 487 34.445 20.161 10.584 1.00 39.75 N ATOM 1852 CA LYS A 487 34.828 20.215 11.976 1.00 38.97 C ATOM 1853 CB LYS A 487 34.122 21.369 12.697 1.00 39.27 C ATOM 1854 CG LYS A 487 34.760 22.719 12.395 1.00 42.48 C ATOM 1855 CD LYS A 487 36.275 22.575 12.241 1.00 45.26 C ATOM 1856 CE LYS A 487 36.953 23.908 12.119 1.00 47.44 C ATOM 1857 NZ LYS A 487 37.048 24.550 13.468 1.00 50.31 N ATOM 1858 C LYS A 487 34.509 18.896 12.637 1.00 38.04 C ATOM 1859 O LYS A 487 35.306 18.390 13.405 1.00 37.61 O ATOM 1860 N LEU A 488 33.354 18.329 12.317 1.00 37.23 N ATOM 1861 CA LEU A 488 32.937 17.098 12.946 1.00 37.18 C ATOM 1862 CB LEU A 488 31.502 16.755 12.561 1.00 36.30 C ATOM 1863 CG LEU A 488 31.030 15.382 12.993 1.00 36.25 C ATOM 1864 CD1 LEU A 488 31.060 15.184 14.496 1.00 37.06 C ATOM 1865 CD2 LEU A 488 29.636 15.172 12.465 1.00 37.46 C ATOM 1866 C LEU A 488 33.885 15.955 12.593 1.00 37.99 C ATOM 1867 O LEU A 488 34.238 15.147 13.466 1.00 37.01 O ATOM 1868 N MET A 489 34.263 15.851 11.317 1.00 38.60 N ATOM 1869 CA MET A 489 35.240 14.828 10.932 1.00 40.07 C ATOM 1870 CB MET A 489 35.412 14.694 9.409 1.00 40.81 C ATOM 1871 CG MET A 489 34.178 14.171 8.704 1.00 44.15 C ATOM 1872 SD MET A 489 33.194 12.913 9.641 1.00 54.88 S ATOM 1873 CE MET A 489 33.908 11.239 9.132 1.00 55.79 C ATOM 1874 C MET A 489 36.572 15.107 11.636 1.00 39.24 C ATOM 1875 O MET A 489 37.216 14.197 12.086 1.00 38.99 O ATOM 1876 N ALA A 490 36.960 16.356 11.813 1.00 39.22 N ATOM 1877 CA ALA A 490 38.226 16.606 12.512 1.00 39.46 C ATOM 1878 CB ALA A 490 38.623 18.062 12.412 1.00 38.63 C ATOM 1879 C ALA A 490 38.152 16.166 13.997 1.00 40.06 C ATOM 1880 O ALA A 490 39.131 15.669 14.568 1.00 40.68 O ATOM 1881 N PHE A 491 36.979 16.351 14.602 1.00 39.40 N ATOM 1882 CA PHE A 491 36.756 15.996 15.982 1.00 38.41 C ATOM 1883 CB PHE A 491 35.449 16.640 16.482 1.00 37.82 C ATOM 1884 CG PHE A 491 35.055 16.218 17.871 1.00 34.23 C ATOM 1885 CD1 PHE A 491 35.515 16.907 18.979 1.00 31.46 C ATOM 1886 CE1 PHE A 491 35.168 16.507 20.263 1.00 31.14 C ATOM 1887 CZ PHE A 491 34.329 15.411 20.445 1.00 29.45 C ATOM 1888 CE2 PHE A 491 33.873 14.724 19.340 1.00 32.47 C ATOM 1889 CD2 PHE A 491 34.233 15.134 18.058 1.00 31.03 C ATOM 1890 C PHE A 491 36.695 14.484 16.112 1.00 39.01 C ATOM 1891 O PHE A 491 37.183 13.910 17.079 1.00 38.94 O ATOM 1892 N LYS A 492 36.077 13.831 15.153 1.00 39.53 N ATOM 1893 CA LYS A 492 35.941 12.401 15.226 1.00 40.55 C ATOM 1894 CB LYS A 492 34.934 11.958 14.192 1.00 40.93 C ATOM 1895 CG LYS A 492 34.730 10.473 14.114 1.00 42.40 C ATOM 1896 CD LYS A 492 33.670 10.118 13.098 1.00 44.01 C ATOM 1897 CE LYS A 492 33.493 8.628 12.999 1.00 44.96 C ATOM 1898 NZ LYS A 492 32.414 8.271 12.044 1.00 47.85 N ATOM 1899 C LYS A 492 37.283 11.668 15.031 1.00 41.46 C ATOM 1900 O LYS A 492 37.425 10.516 15.389 1.00 41.69 O ATOM 1901 N ALA A 493 38.275 12.336 14.476 1.00 42.47 N ATOM 1902 CA ALA A 493 39.570 11.696 14.290 1.00 43.19 C ATOM 1903 CB ALA A 493 40.374 12.445 13.226 1.00 43.14 C ATOM 1904 C ALA A 493 40.340 11.640 15.612 1.00 43.40 C ATOM 1905 O ALA A 493 41.244 10.812 15.802 1.00 44.12 O ATOM 1906 N ILE A 494 39.979 12.516 16.531 1.00 42.66 N ATOM 1907 CA ILE A 494 40.651 12.589 17.806 1.00 42.35 C ATOM 1908 CB ILE A 494 40.873 14.048 18.163 1.00 42.63 C ATOM 1909 CG1 ILE A 494 41.824 14.686 17.155 1.00 44.49 C ATOM 1910 CD1 ILE A 494 41.756 16.198 17.142 1.00 44.88 C ATOM 1911 CG2 ILE A 494 41.451 14.167 19.560 1.00 44.25 C ATOM 1912 C ILE A 494 39.882 11.920 18.942 1.00 41.61 C ATOM 1913 O ILE A 494 40.485 11.551 19.953 1.00 41.78 O ATOM 1914 N TYR A 495 38.566 11.796 18.796 1.00 40.39 N ATOM 1915 CA TYR A 495 37.722 11.225 19.830 1.00 39.98 C ATOM 1916 CB TYR A 495 36.916 12.324 20.513 1.00 39.79 C ATOM 1917 CG TYR A 495 37.731 13.430 21.115 1.00 38.81 C ATOM 1918 CD1 TYR A 495 37.949 14.585 20.415 1.00 38.27 C ATOM 1919 CE1 TYR A 495 38.685 15.600 20.932 1.00 38.45 C ATOM 1920 CZ TYR A 495 39.209 15.508 22.194 1.00 39.44 C ATOM 1921 OH TYR A 495 39.947 16.582 22.669 1.00 40.01 O ATOM 1922 CE2 TYR A 495 39.013 14.366 22.941 1.00 38.56 C ATOM 1923 CD2 TYR A 495 38.260 13.329 22.402 1.00 38.69 C ATOM 1924 C TYR A 495 36.747 10.209 19.257 1.00 40.43 C ATOM 1925 O TYR A 495 35.548 10.290 19.483 1.00 40.56 O ATOM 1926 N PRO A 496 37.255 9.201 18.567 1.00 40.98 N ATOM 1927 CA PRO A 496 36.379 8.261 17.871 1.00 40.62 C ATOM 1928 CB PRO A 496 37.344 7.229 17.288 1.00 41.12 C ATOM 1929 CG PRO A 496 38.747 7.789 17.496 1.00 41.49 C ATOM 1930 CD PRO A 496 38.682 −8.848 18.486 1.00 40.68 C ATOM 1931 C PRO A 496 35.392 7.567 18.796 1.00 40.79 C ATOM 1932 O PRO A 496 34.263 7.261 18.404 1.00 41.69 O ATOM 1933 N ASP A 497 35.814 7.254 20.008 1.00 40.89 N ATOM 1934 CA ASP A 497 34.937 6.528 20.913 1.00 40.80 C ATOM 1935 CB ASP A 497 35.745 5.792 21.988 1.00 41.84 C ATOM 1936 CG ASP A 497 36.300 4.475 21.485 1.00 45.64 C ATOM 1937 OD1 ASP A 497 36.821 3.696 22.320 1.00 53.60 O ATOM 1938 OD2 ASP A 497 36.249 4.124 20.282 1.00 48.70 O ATOM 1939 C ASP A 497 33.902 7.409 21.579 1.00 39.07 C ATOM 1940 O ASP A 497 32.847 6.919 21.956 1.00 38.09 O ATOM 1941 N ILE A 498 34.211 8.697 21.744 1.00 38.14 N ATOM 1942 CA ILE A 498 33.230 9.640 22.273 1.00 37.33 C ATOM 1943 CB ILE A 498 33.864 11.039 22.491 1.00 38.00 C ATOM 1944 CG1 ILE A 498 34.902 11.018 23.627 1.00 39.27 C ATOM 1945 CD1 ILE A 498 34.375 10.559 24.947 1.00 40.90 C ATOM 1946 CG2 ILE A 498 32.797 12.090 22.770 1.00 37.86 C ATOM 1947 C ILE A 498 32.092 9.696 21.272 1.00 36.02 C ATOM 1948 O ILE A 498 30.929 9.572 21.625 1.00 35.72 O ATOM 1949 N VAL A 499 32.429 9.814 20.002 1.00 35.39 N ATOM 1950 CA VAL A 499 31.400 9.915 18.994 1.00 35.49 C ATOM 1951 CB VAL A 499 31.969 10.182 17.580 1.00 34.87 C ATOM 1952 CG1 VAL A 499 30.868 10.168 16.543 1.00 34.58 C ATOM 1953 CG2 VAL A 499 32.686 11.485 17.542 1.00 34.93 C ATOM 1954 C VAL A 499 30.598 8.647 18.975 1.00 35.88 C ATOM 1955 O VAL A 499 29.384 8.684 18.933 1.00 36.02 O ATOM 1956 N ARG A 500 31.278 7.515 19.004 1.00 36.41 N ATOM 1957 CA ARG A 500 30.600 6.237 18.880 1.00 36.86 C ATOM 1958 CB ARG A 500 31.629 5.129 18.714 1.00 37.54 C ATOM 1959 CG ARG A 500 31.058 3.739 18.596 1.00 41.50 C ATOM 1960 CD ARG A 500 32.137 2.639 18.598 1.00 46.56 C ATOM 1961 NE ARG A 500 31.814 1.588 19.576 1.00 51.65 N ATOM 1962 CZ ARG A 500 32.514 1.331 20.688 1.00 52.82 C ATOM 1963 NH1 ARG A 500 33.613 2.013 20.978 1.00 53.74 N ATOM 1964 NH2 ARG A 500 32.117 0.370 21.508 1.00 54.03 N ATOM 1965 C ARG A 500 29.724 5.950 20.066 1.00 36.07 C ATOM 1966 O ARG A 500 28.570 5.586 19.884 1.00 36.22 O ATOM 1967 N LEU A 501 30.247 6.133 21.277 1.00 35.25 N ATOM 1968 CA LEU A 501 29.493 5.780 22.495 1.00 35.10 C ATOM 1969 CB LEU A 501 30.444 5.244 23.602 1.00 35.42 C ATOM 1970 CG LEU A 501 31.187 3.915 23.312 1.00 38.90 C ATOM 1971 CD1 LEU A 501 32.025 3.417 24.493 1.00 41.10 C ATOM 1972 CD2 LEU A 501 30.219 2.807 22.904 1.00 40.70 C ATOM 1973 C LEU A 501 28.609 6.885 23.083 1.00 33.61 C ATOM 1974 O LEU A 501 27.660 6.590 23.788 1.00 32.60 O ATOM 1975 N HIS A 502 28.891 8.152 22.799 1.00 33.08 N ATOM 1976 CA HIS A 502 28.121 9.226 23.475 1.00 32.46 C ATOM 1977 CB HIS A 502 29.049 9.936 24.480 1.00 32.21 C ATOM 1978 CG HIS A 502 29.690 8.993 25.454 1.00 32.45 C ATOM 1979 ND1 HIS A 502 28.998 8.440 26.515 1.00 34.45 N ATOM 1980 CE1 HIS A 502 29.796 7.616 27.175 1.00 33.23 C ATOM 1981 NE2 HIS A 502 30.978 7.610 26.582 1.00 32.06 N ATOM 1982 CD2 HIS A 502 30.940 8.457 25.499 1.00 32.50 C ATOM 1983 C HIS A 502 27.392 10.237 22.575 1.00 31.35 C ATOM 1984 O HIS A 502 26.671 11.084 23.064 1.00 32.31 O ATOM 1985 N PHE A 503 27.572 10.171 21.269 1.00 30.30 N ATOM 1986 CA PHE A 503 26.839 11.071 20.401 1.00 29.71 C ATOM 1987 CB PHE A 503 27.636 11.366 19.123 1.00 28.59 C ATOM 1988 CG PHE A 503 28.589 12.527 19.253 1.00 27.67 C ATOM 1989 CD1 PHE A 503 29.265 12.774 20.443 1.00 28.62 C ATOM 1990 CE1 PHE A 503 30.132 13.869 20.575 1.00 24.57 C ATOM 1991 CZ PHE A 503 30.313 14.715 19.523 1.00 23.93 C ATOM 1992 CE2 PHE A 503 29.635 14.481 18.322 1.00 27.80 C ATOM 1993 CD2 PHE A 503 28.783 13.402 18.194 1.00 27.49 C ATOM 1994 C PHE A 503 25.465 10.483 20.086 1.00 29.88 C ATOM 1995 O PHE A 503 25.301 9.290 20.004 1.00 29.58 O ATOM 1996 N PRO A 504 24.472 11.327 19.887 1.00 30.28 N ATOM 1997 CA PRO A 504 23.131 10.838 19.561 1.00 30.42 C ATOM 1998 CB PRO A 504 22.305 12.107 19.435 1.00 30.02 C ATOM 1999 CG PRO A 504 23.129 13.163 20.095 1.00 30.50 C ATOM 2000 CD PRO A 504 24.559 12.793 19.900 1.00 29.70 C ATOM 2001 C PRO A 504 23.112 10.094 18.232 1.00 30.68 C ATOM 2002 O PRO A 504 23.698 10.533 17.261 1.00 29.79 O ATOM 2003 N PRO A 505 22.410 8.973 18.199 1.00 31.99 N ATOM 2004 CA PRO A 505 22.330 8.126 16.997 1.00 32.55 C ATOM 2005 CB PRO A 505 21.334 7.055 17.397 1.00 32.91 C ATOM 2006 CG PRO A 505 21.520 6.943 18.876 1.00 33.39 C ATOM 2007 CD PRO A 505 21.710 8.384 19.347 1.00 32.17 C ATOM 2008 C PRO A 505 21.866 8.820 15.736 1.00 32.64 C ATOM 2009 O PRO A 505 22.416 8.540 14.662 1.00 33.22 O ATOM 2010 N LEU A 506 20.888 9.709 15.843 1.00 32.69 N ATOM 2011 CA LEU A 506 20.388 10.427 14.673 1.00 32.07 C ATOM 2012 CB LEU A 506 19.117 11.204 15.015 1.00 32.44 C ATOM 2013 CG LEU A 506 18.566 12.012 13.840 1.00 31.16 C ATOM 2014 CD1 LEU A 506 18.156 11.092 12.722 1.00 33.03 C ATOM 2015 CD2 LEU A 506 17.398 12.836 14.302 1.00 32.49 C ATOM 2016 C LEU A 506 21.425 11.369 14.091 1.00 32.28 C ATOM 2017 O LEU A 506 21.491 11.528 12.893 1.00 32.61 O ATOM 2018 N TYR A 507 22.210 12.012 14.949 1.00 32.83 N ATOM 2019 CA TYR A 507 23.327 12.879 14.533 1.00 32.73 C ATOM 2020 CB TYR A 507 23.927 13.589 15.762 1.00 32.18 C ATOM 2021 CG TYR A 507 25.025 14.643 15.516 1.00 30.21 C ATOM 2022 CD1 TYR A 507 24.733 15.980 15.458 1.00 27.51 C ATOM 2023 CE1 TYR A 507 25.715 16.908 15.284 1.00 28.26 C ATOM 2024 CZ TYR A 507 27.020 16.500 15.176 1.00 29.93 C ATOM 2025 OH TYR A 507 28.032 17.414 14.997 1.00 30.78 O ATOM 2026 CE2 TYR A 507 27.336 15.180 15.239 1.00 28.89 C ATOM 2027 CD2 TYR A 507 26.365 14.273 15.423 1.00 29.57 C ATOM 2028 C TYR A 507 24.405 12.054 13.802 1.00 33.67 C ATOM 2029 O TYR A 507 24.928 12.468 12.770 1.00 32.52 O ATOM 2030 N LYS A 508 24.730 10.895 14.351 1.00 35.19 N ATOM 2031 CA LYS A 508 25.674 9.979 13.703 1.00 36.84 C ATOM 2032 CB LYS A 508 25.931 8.740 14.548 1.00 36.89 C ATOM 2033 CG LYS A 508 26.837 8.988 15.763 1.00 38.78 C ATOM 2034 CD LYS A 508 27.446 7.686 16.296 1.00 39.11 C ATOM 2035 CE LYS A 508 26.536 7.042 17.265 1.00 41.23 C ATOM 2036 NZ LYS A 508 27.053 5.702 17.721 1.00 42.04 N ATOM 2037 C LYS A 508 25.165 9.560 12.332 1.00 37.51 C ATOM 2038 O LYS A 508 25.908 9.643 11.386 1.00 37.79 O ATOM 2039 N GLU A 509 23.893 9.165 12.232 1.00 38.63 N ATOM 2040 CA GLU A 509 23.313 8.734 10.968 1.00 39.31 C ATOM 2041 CB GLU A 509 21.863 8.281 11.131 1.00 39.58 C ATOM 2042 CG GLU A 509 21.670 6.932 11.815 1.00 44.44 C ATOM 2043 CD GLU A 509 20.198 6.514 11.993 1.00 48.40 C ATOM 2044 OE1 GLU A 509 19.956 5.642 12.854 1.00 52.15 O ATOM 2045 OE2 GLU A 509 19.285 7.028 11.285 1.00 50.58 O ATOM 2046 C GLU A 509 23.333 9.841 9.937 1.00 39.53 C ATOM 2047 O GLU A 509 23.504 9.571 8.745 1.00 39.45 O ATOM 2048 N LEU A 510 23.126 11.083 10.379 1.00 39.18 N ATOM 2049 CA LEU A 510 23.067 12.201 9.456 1.00 39.07 C ATOM 2050 CB LEU A 510 22.226 13.338 10.040 1.00 39.33 C ATOM 2051 CG LEU A 510 20.725 13.091 10.200 1.00 39.95 C ATOM 2052 CD1 LEU A 510 20.091 14.296 10.800 1.00 41.52 C ATOM 2053 CD2 LEU A 510 20.058 12.768 8.899 1.00 40.94 C ATOM 2054 C LEU A 510 24.401 12.783 9.030 1.00 38.89 C ATOM 2055 O LEU A 510 24.503 13.334 7.943 1.00 39.03 O ATOM 2056 N PHE A 511 25.427 12.680 9.854 1.00 38.62 N ATOM 2057 CA PHE A 511 26.619 13.464 9.591 1.00 38.51 C ATOM 2058 CB PHE A 511 26.736 14.569 10.646 1.00 38.47 C ATOM 2059 CG PHE A 511 25.542 15.483 10.711 1.00 39.17 C ATOM 2060 CD1 PHE A 511 24.848 15.663 11.910 1.00 37.90 C ATOM 2061 CE1 PHE A 511 23.762 16.508 11.985 1.00 37.16 C ATOM 2062 CZ PHE A 511 23.324 17.165 10.866 1.00 39.02 C ATOM 2063 CE2 PHE A 511 24.005 16.998 9.653 1.00 39.88 C ATOM 2064 CD2 PHE A 511 25.113 16.167 9.587 1.00 40.32 C ATOM 2065 C PHE A 511 27.915 12.682 9.565 1.00 38.68 C ATOM 2066 O PHE A 511 28.923 13.297 9.211 1.00 38.22 O ATOM 2067 OXT PHE A 511 27.963 11.489 9.895 1.00 39.77 O ATOM 2068 C65 CHS L 1 29.670 21.352 16.280 1.00 40.20 C ATOM 2069 C63 CHS L 1 28.173 21.713 16.502 1.00 35.49 C ATOM 2070 C69 CHS L 1 27.552 20.583 17.354 1.00 36.38 C ATOM 2071 C60 CHS L 1 28.076 23.102 17.181 1.00 33.50 C ATOM 2072 C57 CHS L 1 26.755 23.921 17.026 1.00 29.77 C ATOM 2073 C54 CHS L 1 26.543 24.885 18.224 1.00 26.05 C ATOM 2074 C48 CHS L 1 25.339 25.868 18.122 1.00 27.06 C ATOM 2075 C50 CHS L 1 25.416 26.630 16.786 1.00 30.39 C ATOM 2076 C38 CHS L 1 23.999 25.113 18.108 1.00 27.35 C ATOM 2077 C35 CHS L 1 23.898 24.161 19.333 1.00 25.32 C ATOM 2078 C29 CHS L 1 22.637 25.885 18.088 1.00 25.81 C ATOM 2079 C25 CHS L 1 22.075 26.442 16.760 1.00 25.48 C ATOM 2080 C40 CHS L 1 22.674 27.065 19.089 1.00 24.66 C ATOM 2081 C30 CHS L 1 21.683 24.733 18.480 1.00 24.66 C ATOM 2082 C32 CHS L 1 22.378 23.988 19.639 1.00 25.34 C ATOM 2083 C18 CHS L 1 20.267 25.269 18.823 1.00 24.65 C ATOM 2084 C15 CHS L 1 19.389 24.126 19.379 1.00 27.21 C ATOM 2085 C20 CHS L 1 19.656 25.910 17.559 1.00 25.94 C ATOM 2086 C23 CHS L 1 20.616 26.987 16.956 1.00 25.70 C ATOM 2087 C22 CHS L 1 18.195 26.423 17.788 1.00 25.96 C ATOM 2088 C44 CHS L 1 18.216 27.828 18.461 1.00 23.41 C ATOM 2089 C12 CHS L 1 17.391 25.437 18.627 1.00 27.66 C ATOM 2090 C9 CHS L 1 15.878 25.602 18.705 1.00 27.52 C ATOM 2091 C13 CHS L 1 17.928 24.439 19.343 1.00 28.47 C ATOM 2092 C1 CHS L 1 17.457 26.540 16.432 1.00 24.95 C ATOM 2093 C4 CHS L 1 15.966 26.932 16.596 1.00 25.61 C ATOM 2094 C7 CHS L 1 15.184 25.850 17.366 1.00 27.22 C ATOM 2095 O6 CHS L 1 13.884 26.323 17.783 1.00 33.31 O ATOM 2096 S1 CHS L 1 12.600 26.109 16.995 1.00 36.30 S ATOM 2097 O3 CHS L 1 11.492 26.689 17.749 1.00 35.79 O ATOM 2098 O2 CHS L 1 12.386 24.736 16.612 1.00 34.23 O ATOM 2099 O4 CHS L 1 12.791 26.916 15.768 1.00 31.69 O ATOM 2100 O HOH V 1 34.374 18.778 31.636 1.00 24.18 O ATOM 2101 O HOH V 2 13.751 22.827 14.717 1.00 25.05 O ATOM 2102 O HOH V 3 17.585 18.928 1.035 1.00 25.61 O ATOM 2103 O HOH V 4 19.468 24.062 23.227 1.00 25.84 O ATOM 2104 O HOH V 5 28.242 16.854 27.596 1.00 28.05 O ATOM 2105 O HOH V 6 26.219 37.914 34.970 1.00 28.23 O ATOM 2106 O HOH V 7 25.424 34.243 27.348 1.00 29.16 O ATOM 2107 O HOH V 8 37.940 8.815 22.096 1.00 29.22 O ATOM 2108 O HOH V 9 34.532 27.583 19.498 1.00 30.78 O ATOM 2109 O HOH V 10 36.533 26.810 13.236 1.00 30.95 O ATOM 2110 O HOH V 11 19.929 34.372 33.559 1.00 31.12 O ATOM 2111 O HOH V 12 30.464 36.924 16.913 1.00 32.33 O ATOM 2112 O HOH V 13 39.694 19.997 26.277 1.00 32.46 O ATOM 2113 O HOH V 14 10.618 25.915 9.224 1.00 33.09 O ATOM 2114 O HOH V 15 19.089 15.060 21.458 1.00 33.35 O ATOM 2115 O HOH V 16 19.982 38.502 24.574 1.00 33.56 O ATOM 2116 O HOH V 17 29.188 18.773 31.889 1.00 34.82 O ATOM 2117 O HOH V 18 32.816 26.367 25.939 1.00 35.28 O ATOM 2118 O HOH V 19 21.757 13.531 27.380 1.00 35.38 O ATOM 2119 O HOH V 20 21.923 18.531 7.233 1.00 35.96 O ATOM 2120 O HOH V 21 33.494 32.602 17.864 1.00 36.22 O ATOM 2121 O HOH V 22 29.529 39.171 20.916 1.00 36.73 O ATOM 2122 O HOH V 23 26.956 19.335 8.080 1.00 37.09 O ATOM 2123 O HOH V 24 17.942 26.092 21.769 1.00 37.19 O ATOM 2124 O HOH V 25 30.129 36.843 14.123 1.00 37.60 O ATOM 2125 O HOH V 26 26.979 35.078 38.228 1.00 37.66 O ATOM 2126 O HOH V 27 11.702 12.320 −11.449 1.00 37.83 O ATOM 2127 O HOH V 28 24.019 40.426 26.459 1.00 38.20 O ATOM 2128 O HOH V 29 32.889 38.167 8.976 1.00 38.30 O ATOM 2129 O HOH V 30 26.368 37.122 27.563 1.00 38.38 O ATOM 2130 O HOH V 31 26.038 37.728 37.444 1.00 38.65 O ATOM 2131 O HOH V 32 −0.184 22.111 6.895 1.00 38.91 O ATOM 2132 O HOH V 33 24.132 19.988 −1.108 1.00 39.60 O ATOM 2133 O HOH V 34 17.228 26.642 24.728 1.00 39.66 O ATOM 2134 O HOH V 35 24.430 17.401 −1.616 1.00 40.07 O ATOM 2135 O HOH V 36 14.466 37.465 9.931 1.00 40.09 O ATOM 2136 O HOH V 37 38.590 23.562 23.909 1.00 40.15 O ATOM 2137 O HOH V 38 20.064 26.866 31.634 1.00 40.16 O ATOM 2138 O HOH V 39 5.285 36.507 11.739 1.00 40.86 O ATOM 2139 O HOH V 40 5.515 30.530 16.484 1.00 40.87 O ATOM 2140 O HOH V 41 24.115 12.660 27.541 1.00 40.92 O ATOM 2141 O HOH V 42 23.756 5.602 14.704 1.00 41.17 O ATOM 2142 O HOH V 43 10.524 40.707 27.825 1.00 41.34 O ATOM 2143 O HOH V 44 26.115 7.036 20.648 1.00 41.58 O ATOM 2144 O HOH V 45 22.909 14.371 0.739 1.00 41.86 O ATOM 2145 O HOH V 46 38.001 12.389 26.816 1.00 42.12 O ATOM 2146 O HOH V 47 27.038 38.349 22.646 1.00 42.13 O ATOM 2147 O HOH V 48 27.926 38.210 14.696 1.00 42.24 O ATOM 2148 O HOH V 49 19.208 17.322 27.275 1.00 42.36 O ATOM 2149 O HOH V 50 17.702 22.996 26.002 1.00 42.43 O ATOM 2150 O HOH V 51 21.518 40.403 26.071 1.00 42.44 O ATOM 2151 O HOH V 52 29.008 37.276 26.773 1.00 42.97 O ATOM 2152 O HOH V 53 16.797 40.023 17.063 1.00 43.20 O ATOM 2153 O HOH V 54 27.959 18.192 30.078 1.00 43.25 O ATOM 2154 O HOH V 55 27.189 38.094 30.644 1.00 43.31 O ATOM 2155 O HOH V 56 32.853 5.119 27.654 1.00 43.36 O ATOM 2156 O HOH V 57 25.498 15.066 28.345 1.00 43.59 O ATOM 2157 O HOH V 58 26.277 3.798 24.349 1.00 43.69 O ATOM 2158 O HOH V 59 24.431 4.474 16.791 1.00 43.83 O ATOM 2159 O HOH V 60 17.931 21.585 22.061 1.00 43.86 O ATOM 2160 O HOH V 61 3.622 36.866 6.230 1.00 43.90 O ATOM 2161 O HOH V 62 29.565 0.033 25.439 1.00 44.03 O ATOM 2162 O HOH V 63 37.471 27.196 26.904 1.00 44.11 O ATOM 2163 O HOH V 64 14.114 35.615 19.648 1.00 44.14 O ATOM 2164 O HOH V 65 32.375 30.570 3.935 1.00 44.29 O ATOM 2165 O HOH V 66 23.674 14.801 −1.168 1.00 44.29 O ATOM 2166 O HOH V 67 10.607 41.218 4.126 1.00 44.59 O ATOM 2167 O HOH V 68 5.553 22.195 −4.232 1.00 45.31 O ATOM 2168 O HOH V 69 18.683 8.716 −3.851 1.00 45.45 O ATOM 2169 O HOH V 70 31.216 36.554 23.614 1.00 45.65 O ATOM 2170 O HOH V 71 32.042 38.382 12.898 1.00 45.78 O ATOM 2171 O HOH V 72 41.571 18.538 20.942 1.00 45.85 O ATOM 2172 O HOH V 73 24.529 18.718 30.164 1.00 45.93 O ATOM 2173 O HOH V 74 12.539 36.492 16.322 1.00 45.97 O ATOM 2174 O HOH V 75 41.603 15.767 13.285 1.00 46.25 O ATOM 2175 O HOH V 76 21.193 17.911 28.154 1.00 46.47 O ATOM 2176 O HOH V 77 29.518 22.554 36.275 1.00 46.60 O ATOM 2177 O HOH V 78 32.636 35.308 17.598 1.00 47.00 O ATOM 2178 O HOH V 79 13.479 40.537 21.946 1.00 47.13 O ATOM 2179 O HOH V 80 32.129 25.488 3.702 1.00 47.21 O ATOM 2180 O HOH V 81 5.317 15.523 10.878 1.00 47.24 O ATOM 2181 O HOH V 82 14.590 12.994 −13.138 1.00 47.42 O ATOM 2182 O HOH V 83 31.688 18.521 32.632 1.00 47.42 O ATOM 2183 O HOH V 84 17.527 41.724 24.627 1.00 47.58 O ATOM 2184 O HOH V 85 2.758 27.645 −6.136 1.00 47.76 O ATOM 2185 O HOH V 86 39.479 15.402 9.361 1.00 47.77 O ATOM 2186 O HOH V 87 27.097 39.457 7.716 1.00 47.80 O ATOM 2187 O HOH V 88 14.854 38.493 18.833 1.00 48.18 O ATOM 2188 O HOH V 89 16.442 28.965 31.902 1.00 48.22 O ATOM 2189 O HOH V 90 6.592 18.094 16.102 1.00 48.28 O ATOM 2190 O HOH V 91 25.862 43.114 20.667 1.00 48.28 O ATOM 2191 O HOH V 92 25.820 31.283 38.083 1.00 48.37 O ATOM 2192 O HOH V 93 21.448 8.215 −6.909 1.00 48.43 O ATOM 2193 O HOH V 94 30.315 7.953 13.447 1.00 48.47 O ATOM 2194 O HOH V 95 11.333 3.609 −1.448 1.00 48.50 O ATOM 2195 O HOH V 96 25.475 26.684 −3.988 1.00 48.54 O ATOM 2196 O HOH V 97 21.825 7.068 6.249 1.00 48.57 O ATOM 2197 O HOH V 98 26.277 39.627 9.743 1.00 48.67 O ATOM 2198 O HOH V 99 10.637 33.053 31.840 1.00 48.70 O ATOM 2199 O HOH V 100 8.248 10.674 15.177 1.00 48.90 O ATOM 2200 O HOH V 101 5.925 25.750 18.970 1.00 48.97 O ATOM 2201 O HOH V 102 15.403 29.322 −7.859 1.00 49.09 O ATOM 2202 O HOH V 103 3.536 35.057 9.239 1.00 49.16 O ATOM 2203 O HOH V 104 24.615 19.046 6.759 1.00 49.20 O ATOM 2204 O HOH V 105 26.458 22.354 32.348 1.00 49.22 O ATOM 2205 O HOH V 106 29.329 9.438 8.558 1.00 49.24 O ATOM 2206 O HOH V 107 38.968 26.081 25.260 1.00 49.30 O ATOM 2207 O HOH V 108 33.166 31.078 20.463 1.00 49.55 O ATOM 2208 O HOH V 109 23.661 41.348 9.046 1.00 49.57 O ATOM 2209 O HOH V 110 −1.905 38.422 −2.103 1.00 49.58 O ATOM 2210 O HOH V 111 23.567 25.829 32.172 1.00 49.84 O ATOM 2211 O HOH V 112 39.174 28.173 18.167 1.00 49.89 O ATOM 2212 O HOH V 113 6.546 17.330 −8.809 1.00 50.15 O ATOM 2213 O HOH V 114 15.378 36.610 16.329 1.00 50.24 O ATOM 2214 O HOH V 115 24.014 21.545 30.393 1.00 50.25 O ATOM 2215 O HOH V 116 13.119 40.412 25.848 1.00 50.51 O ATOM 2216 O HOH V 117 34.344 32.657 10.572 1.00 50.99 O ATOM 2217 O HOH V 118 26.462 26.162 35.827 1.00 51.01 O ATOM 2218 O HOH V 119 37.119 20.213 15.138 1.00 51.01 O ATOM 2219 O HOH V 120 20.402 7.809 0.264 1.00 51.21 O ATOM 2220 O HOH V 121 32.907 23.096 33.511 1.00 51.26 O ATOM 2221 O HOH V 122 18.316 15.239 25.933 1.00 51.36 O ATOM 2222 O HOH V 123 22.210 27.272 33.235 1.00 51.39 O ATOM 2223 O HOH V 124 4.773 34.446 −7.751 1.00 51.56 O ATOM 2224 O HOH V 125 −11.176 24.480 −12.026 1.00 51.70 O ATOM 2225 O HOH V 126 29.201 40.901 16.488 1.00 51.72 O ATOM 2226 O HOH V 127 −14.169 32.191 −15.792 1.00 51.83 O ATOM 2227 O HOH V 128 27.174 21.751 2.087 1.00 51.83 O ATOM 2228 O HOH V 129 12.661 30.921 30.244 1.00 51.89 O ATOM 2229 O HOH V 130 16.175 21.212 25.031 1.00 51.93 O ATOM 2230 O HOH V 131 20.211 40.398 29.373 1.00 52.00 O ATOM 2231 O HOH V 132 −13.899 29.982 −18.098 1.00 52.10 O ATOM 2232 O HOH V 133 15.844 9.719 16.408 1.00 52.40 O ATOM 2233 O HOH V 134 31.386 39.552 17.146 1.00 52.59 O ATOM 2234 O HOH V 135 0.640 32.016 4.846 1.00 52.62 O ATOM 2235 O HOH V 136 42.270 20.847 16.516 1.00 52.68 O ATOM 2236 O HOH V 137 17.490 42.697 21.680 1.00 52.79 O ATOM 2237 O HOH V 138 29.839 40.760 8.920 1.00 52.82 O ATOM 2238 O HOH V 139 4.290 30.109 9.865 1.00 52.89 O ATOM 2239 O HOH V 140 19.892 7.267 −2.229 1.00 53.00 O ATOM 2240 O HOH V 141 9.212 35.423 31.648 1.00 53.10 O ATOM 2241 O HOH V 142 31.957 28.820 37.099 1.00 53.23 O ATOM 2242 O HOH V 143 40.970 31.344 14.438 1.00 53.27 O ATOM 2243 O HOH V 144 40.782 22.485 20.153 1.00 53.41 O ATOM 2244 O HOH V 145 4.688 33.007 −12.475 1.00 53.62 O ATOM 2245 O HOH V 146 12.405 42.730 −6.583 1.00 53.65 O ATOM 2246 O HOH V 147 30.118 41.753 23.343 1.00 53.90 O ATOM 2247 O HOH V 148 40.310 19.731 15.626 1.00 54.03 O ATOM 2248 O HOH V 149 9.904 10.991 −10.125 1.00 54.05 O ATOM 2249 O HOH V 150 35.645 26.966 10.324 1.00 54.10 O ATOM 2250 O HOH V 151 3.249 13.849 9.818 1.00 54.12 O ATOM 2251 O HOH V 152 8.994 41.917 8.500 1.00 54.13 O ATOM 2252 O HOH V 153 25.494 7.351 8.323 1.00 54.13 O ATOM 2253 O HOH V 154 −19.853 30.788 −6.983 1.00 54.14 O ATOM 2254 O HOH V 155 28.190 2.825 26.243 1.00 54.20 O ATOM 2255 O HOH V 156 14.754 37.385 13.109 1.00 54.33 O ATOM 2256 O HOH V 157 13.944 9.467 −11.887 1.00 54.33 O ATOM 2257 O HOH V 158 5.602 27.878 16.557 1.00 54.52 O ATOM 2258 O HOH V 159 35.605 5.102 13.754 1.00 54.70 O ATOM 2259 O HOH V 160 24.308 35.094 −1.504 1.00 54.70 O ATOM 2260 O HOH V 161 28.337 18.154 4.417 1.00 54.85 O ATOM 2261 O HOH V 162 34.895 34.791 30.514 1.00 54.94 O ATOM 2262 O HOH V 163 4.910 16.781 14.763 1.00 55.00 O ATOM 2263 O HOH V 164 11.023 5.038 5.200 1.00 55.13 O ATOM 2264 O HOH V 165 39.542 17.117 25.841 1.00 55.21 O ATOM 2265 O HOH V 166 24.386 37.780 −6.091 1.00 55.24 O ATOM 2266 O HOH V 167 20.889 19.941 29.200 1.00 55.34 O ATOM 2267 O HOH V 168 6.752 22.057 −14.805 1.00 55.38 O ATOM 2268 O HOH V 169 25.163 5.963 12.276 1.00 55.50 O ATOM 2269 O HOH V 170 28.609 39.754 12.521 1.00 55.51 O ATOM 2270 O HOH V 171 11.031 13.390 14.244 1.00 55.56 O ATOM 2271 O HOH V 172 24.662 35.439 2.257 1.00 55.60 O ATOM 2272 O HOH V 173 36.161 34.403 25.458 1.00 55.61 O ATOM 2273 O HOH V 174 9.631 6.595 3.959 1.00 55.62 O ATOM 2274 O HOH V 175 38.038 17.337 8.038 1.00 55.79 O ATOM 2275 O HOH V 176 0.834 36.938 9.105 1.00 55.88 O ATOM 2276 O HOH V 177 30.977 6.285 15.282 1.00 55.89 O ATOM 2277 O HOH V 178 36.456 34.296 14.233 1.00 55.99 O ATOM 2278 O HOH V 179 −16.740 27.510 −6.376 1.00 56.17 O ATOM 2279 O HOH V 180 17.830 28.498 −7.217 1.00 56.32 O ATOM 2280 O HOH V 181 27.092 42.066 23.041 1.00 56.37 O ATOM 2281 O HOH V 182 32.854 20.918 3.041 1.00 56.40 O ATOM 2282 O HOH V 183 33.531 36.555 20.279 1.00 56.52 O ATOM 2283 O HOH V 184 29.161 9.790 11.459 1.00 56.74 O ATOM 2284 O HOH V 185 30.947 21.061 33.802 1.00 56.78 O ATOM 2285 O HOH V 186 4.419 10.917 12.329 1.00 57.20 O ATOM 2286 O HOH V 187 35.731 21.349 33.562 1.00 57.25 O ATOM 2287 O HOH V 188 10.127 34.435 −7.921 1.00 57.31 O ATOM 2288 O HOH V 189 24.815 39.636 5.433 1.00 57.31 O ATOM 2289 O HOH V 190 16.135 28.959 −10.450 1.00 57.40 O ATOM 2290 O HOH V 191 28.755 27.074 −0.804 1.00 57.58 O ATOM 2291 O HOH V 192 37.694 28.335 20.845 1.00 58.09 O ATOM 2292 O HOH V 193 12.094 17.839 22.662 1.00 58.11 O ATOM 2293 O HOH V 194 16.739 12.034 −12.326 1.00 58.15 O ATOM 2294 O HOH V 195 35.658 34.834 39.271 1.00 58.17 O ATOM 2295 O HOH V 196 6.325 23.731 −10.962 1.00 58.22 O ATOM 2296 O HOH V 197 40.239 32.219 19.158 1.00 58.22 O ATOM 2297 O HOH V 198 42.009 17.600 28.618 1.00 58.40 O ATOM 2298 O HOH V 199 13.977 43.767 4.977 1.00 58.43 O ATOM 2299 O HOH V 200 16.099 2.261 −8.711 1.00 58.43 O ATOM 2300 O HOH V 201 28.967 4.492 15.572 1.00 58.44 O ATOM 2301 O HOH V 202 −9.860 29.231 −7.273 1.00 58.50 O ATOM 2302 O HOH V 203 19.071 45.087 23.986 1.00 58.89 O ATOM 2303 O HOH V 204 23.529 32.968 −5.882 1.00 59.37 O ATOM 2304 O HOH V 205 42.799 19.843 29.263 1.00 59.50 O ATOM 2305 O HOH V 206 21.137 24.412 31.357 1.00 59.65 O ATOM 2306 O HOH V 207 21.855 22.367 32.296 1.00 59.84 O ATOM 2307 O HOH V 208 3.008 31.149 11.774 1.00 59.88 O ATOM 2308 O HOH V 209 25.290 39.928 29.735 1.00 59.89 O ATOM 2309 O HOH V 210 20.546 26.076 −5.981 1.00 60.27 O ATOM 2310 O HOH V 211 7.922 7.232 −0.636 1.00 60.32 O ATOM 2311 O HOH V 212 7.268 35.864 −11.540 1.00 60.42 O ATOM 2312 O HOH V 213 5.789 26.044 −10.740 1.00 60.43 O ATOM 2313 O HOH V 214 26.552 14.136 −0.935 1.00 60.54 O ATOM 2314 O HOH V 215 41.103 32.645 22.002 1.00 60.87 O ATOM 2315 O HOH V 216 10.211 45.156 8.475 1.00 61.19 O ATOM 2316 O HOH V 217 25.176 9.626 5.053 1.00 61.26 O ATOM 2317 O HOH V 218 11.154 41.223 20.664 1.00 61.36 O ATOM 2318 O HOH V 219 12.673 39.495 16.829 1.00 61.48 O ATOM 2319 O HOH V 220 6.931 21.130 20.882 1.00 61.81 O ATOM 2320 O HOH V 221 34.324 35.314 27.782 1.00 61.99 O ATOM 2321 O HOH V 222 22.533 27.773 −4.889 1.00 62.36 O ATOM 2322 O HOH V 223 26.615 24.563 −3.514 1.00 62.43 O ATOM 2323 O HOH V 224 22.620 8.612 −0.252 1.00 62.66 O ATOM 2324 O HOH V 225 7.850 40.686 5.273 1.00 62.89 O ATOM 2325 O HOH V 226 13.072 10.222 19.270 1.00 62.97 O ATOM 2326 O HOH V 227 36.863 23.365 8.281 1.00 63.29 O ATOM 2327 O HOH V 228 3.086 21.555 0.662 1.00 63.45 O ATOM 2328 O HOH V 229 40.090 16.185 28.416 1.00 63.62 O ATOM 2329 O HOH V 230 28.499 41.692 20.652 1.00 63.74 O ATOM 2330 O HOH V 231 5.053 21.524 −0.933 1.00 63.76 O ATOM 2331 O HOH V 232 18.279 22.767 −9.711 1.00 63.86 O ATOM 2332 O HOH V 233 4.021 13.207 14.475 1.00 64.13 O ATOM 2333 O HOH V 234 20.707 46.785 18.023 1.00 64.17 O ATOM 2334 O HOH V 235 18.269 24.266 −5.185 1.00 64.61 O ATOM 2335 O HOH V 236 −1.075 31.083 6.459 1.00 64.71 O ATOM 2336 O HOH V 237 36.067 6.771 10.766 1.00 64.72 O ATOM 2337 O HOH V 238 41.379 11.059 22.312 1.00 64.85 O ATOM 2338 O HOH V 239 2.764 21.069 −4.139 1.00 64.89 O ATOM 2339 O HOH V 240 36.774 12.493 29.500 1.00 64.91 O ATOM 2340 O HOH V 241 33.576 7.054 15.865 1.00 65.14 O ATOM 2341 O HOH V 242 14.783 25.737 26.607 1.00 65.39 O ATOM 2342 O HOH V 243 19.632 29.934 −8.079 1.00 65.40 O ATOM 2343 O HOH V 244 19.893 42.353 12.315 1.00 65.64 O ATOM 2344 O HOH V 245 30.511 40.345 32.883 1.00 66.15 O ATOM 2345 O HOH V 246 6.494 31.838 −13.514 1.00 66.20 O ATOM 2346 O HOH V 247 41.592 29.824 26.952 1.00 67.14 O ATOM 2347 O HOH V 248 10.095 12.965 −13.010 1.00 68.08 O ATOM 2348 O HOH V 249 28.076 13.999 7.164 1.00 68.53 O ATOM 2349 O HOH V 250 16.142 3.364 3.323 1.00 68.80 O ATOM 2350 O HOH V 251 11.453 41.019 −1.487 1.00 68.99 O ATOM 2351 O HOH V 252 22.049 30.697 36.943 1.00 69.14 O ATOM 2352 O HOH V 253 31.306 29.631 39.320 1.00 69.25 O ATOM 2353 O HOH V 254 26.120 35.578 0.298 1.00 69.34 O ATOM 2354 O HOH V 255 37.240 33.402 37.433 1.00 69.56 O ATOM 2355 O HOH V 256 14.450 19.763 22.059 1.00 70.09 O 

1. Crystalline LBD of RORα.
 2. The crystalline LBD of RORα of claim 1 wherein said LBD of RORα is associated with a small molecule.
 3. The crystalline LBD of RORα of claim 1 wherein said LBD of RORα is associated with a lipophilic substance.
 4. The crystalline LBD of RORα of claim 2 wherein said lipophilic substance is cholesterol or a derivative of cholesterol.
 5. The crystalline LBD of RORα of claim 1 wherein said crystal comprises a unit cell having the dimensions of a=55.9 Å±2 Å, b=49.9 Å±2 Å, c=60.7 Å±2 Å and β=98.70°±5°and space group P2(1).
 6. The crystalline LBD of RORα of claim 1 wherein said crystalline LBD of RORα comprises the atomic structure coordinates of Table 8 or 9 or a part thereof.
 7. A heavy atom derivative of a crystal according to claim
 1. 8. A computer readable medium comprising a model embodying the structure of the LBD RORα comprising one or more sets of atomic coordinates in Table 8 or
 9. 9. A method for identifying a substance binding to the LBD of RORα, comprising: (a) contacting a candidate substance with a model embodying the structure of the LBD of RORα comprising one or more sets of atomic coordinates in Table 8 or 9; (b) assessing the interaction of said candidate substance with said model, and; (c) selecting a substance which is predicted to interact with the LED of RORα.
 10. (canceled)
 11. A method according to claim 9 wherein the substance interacts directly or indirectly with one or more amino acids selected from the group consisting of: Cys321, Gln322, Tyr323, Leu328,Trp353, Cys356, Ala357, Lys359, Ile360, Glu362,Ala363, Val397, Phe398, Arg400, Met401, Arg403, Ala404, Val412, Tyr413, Phe414, Phe424, Leu427, Cys429, Phe432, Ile433, Val436, His517, Lys520 and Tyr540.
 12. A method according to claim 9 wherein the substance interacts directly or indirectly with one or more amino acids selected from the group consisting of: Gln322, Tyr323, Arg400 and Arg403.
 13. A method according to claim 9 using a homologue of said model, wherein said homologue has a root mean square derivation from the backbone atoms of said amino acids of not more than 1.5 Å.
 14. The method of claim 9 wherein the substance is a small molecule.
 15. The method of claim 14 wherein said substance is cholesterol or a cholesterol derivative.
 16. A method for identifying an agonist or antagonist that binds to the LBD of RORα comprising: (a) selecting a potential compound by performing rational drug design with one or more sets of atomic coordinates set forth in Table 8 or 9, wherein said selecting is performed in conjunction with computer modeling; (b) contacting the potential compound with a LBD of RORα and (c) measuring the biological activity of RORα.
 17. The method of claim 16 wherein said compound is designed to interact directly or indirectly with one or more amino acids selected from the group consisting of: Cys321, Gln322, Tyr323, Leu328,Trp353, Cys356, Ala357, Lys359, Ile360, Glu362, Ala363, Val397, Phe398, Arg400, Met401, Arg403, Ala404, Val412, Tyr413, Phe414, Phe424, Leu427, Cys429, Phe432, Ile433, Val436, His517, Lys520 and Tyr540.
 18. A method according to claim 17 wherein the substance interacts directly or indirectly with one or more amino acids selected from the group consisting of: Gln322, Tyr323, Arg400 and Arg403.
 19. The method of claim 18 wherein said compound is selected as RORα agonist if it stabilizes helix 12 of the LBD of RORα in the agonist position.
 20. The method of claim 19 wherein said compound is selected as RORα antagonist if it destabilizes helix 12 of the LBD of RORα from the agonist position.
 21. A pharmaceutical composition comprising a therapeutically effective amount of a compound stabilizing helix 12 of RORα in the agonist position and a pharmaceutically acceptable carrier.
 22. A pharmaceutical composition comprising a therapeutically effective amount of a compound destabilizing helix 12 of RORα from the agonist position and a pharmaceutically acceptable carrier.
 23. A method of screening for compounds interacting with RORα comprising: (a) contacting RORα with a candidate compound, (b) measuring interactions between the candidate compound and RORα in the absence of sterols, and (c) selecting said compound if it interacts with RORα.
 24. The method of claim 23 for the screening for compounds useful for the treatment of cholesterol related diseases.
 25. The method of claim 23 for the screening for compounds useful for the treatment of endocrine disorders, atherosclerosis and cardiovascular diseases, metabolic diseases such as for instance obesity, inflammatory diseases, skin diseases, diseases related to the CNS, such as for instance Alzheimer disease and tumor related diseases.
 26. Use of RORα in cellular screening assays for the identification of compounds useful for the treatment of cholesterol related diseases.
 27. Use of RORα in cellular screening assays for the identification of compounds with endocrine disorders, atherosclerosis and cardiovascular diseases, metabolic diseases such as for instance obesity, inflammatory diseases, skin diseases, diseases related to the CNS, such as for instance Alzheimer disease and tumor related diseases.
 28. A composition comprising LBD of RORα and cholesterol or a cholesterol derivative.
 29. A composition according to claim 28 wherein said composition is crystallizable.
 30. The crystalline LBD of RORα of claim 2 wherein said LBD of RORα is associated with a lipophilic substance.
 31. The crystalline LBD of RORα of claim 2 wherein said crystal comprises a unit cell having the dimensions of a=55.9 Å±2 Å,b=49.9 Å±2 Å, c=60.7 Å±2 Å and β=98.7±5° and space groupP2(1).
 32. The crystalline LBD of RORα of claim 3 wherein said crystal comprises a unit cell having the dimensions of a=55.9 Å±2 Å, b=49.9 Å±2 Å, c=60.7 Å±2 Å and β=98.7°±5° and space groupP2(1).
 33. The crystalline LBD of RORα of claim 2 wherein said crystalline LBD of RORα comprises the atomic structure coordinates of Table 8 or 9 or a part thereof.
 34. The crystalline LBD of RORα of claim 3 wherein said crystalline LBD of RORα comprises the atomic structure coordinates of Table 8 or 9 or a part thereof.
 35. A heavy atom derivative of a crystal according to claim
 2. 36. A heavy atom derivative of a crystal according to claim
 3. 37. A heavy atom derivative of a crystal according to claim
 31. 38. A heavy atom derivative of a crystal according to claim
 32. 39. A heavy atom derivative of a crystal according to claim
 33. 40. A heavy atom derivative of a crystal according to claim
 34. 